J. Klinman

发表

Climate change and the integrity of science.

G. B. Dalrymple, W. R. Gardner, R. Rivest, 2010, Science.

Nature of rate-limiting steps in a compartmentalized enzyme system. Quantitation of dopamine transport and hydroxylation rates in resealed chromaffin granule ghosts.

J. Klinman, N. Ahn, 1989, Journal of Biological Chemistry.

Erratum: Ribosomally synthesized and post-translationally modified peptide natural products: Overview and recommendations for a universal nomenclature (Natural Product Reports (2013) 30 (108-160) DOI:10.1039/C2NP20085F)

P. G. Arnison, M. Bibb, B. Shen, 2013 .

Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.

P. G. Arnison, M. Bibb, B. Shen, 2013, Natural product reports.

Hydrogen tunneling in enzyme reactions.

C. J. Murray, J. Klinman, Y. Cha, 1989, Science.

Extremely Large Isotope Effects in the Soybean Lipoxygenase-Linoleic Acid Reaction

J. Klinman, M. Glickman, J. Wiseman, 1994 .

Nature of hydrogen transfer in soybean lipoxygenase 1: separation of primary and secondary isotope effects.

J. Klinman, K. Rickert, 1999, Biochemistry.

Tunneling and dynamics in enzymatic hydride transfer.

J. Klinman, Z. Nagel, 2006, Chemical reviews.

Biophysical Characterization of a Disabled Double Mutant of Soybean Lipoxygenase: The "Undoing" of Precise Substrate Positioning Relative to Metal Cofactor and an Identified Dynamical Network.

E. M. Thompson, J. Klinman, C. Gee, 2019, Journal of the American Chemical Society.

At the confluence of ribosomally synthesized peptide modification and radical S-adenosylmethionine (SAM) enzymology

J. Klinman, J. Latham, Ian Barr, 2017, The Journal of Biological Chemistry.

The pyrroloquinoline quinone ( PQQ ) biosynthetic pathway : Demonstration of de novo carbon-carbon cross-linking within the peptide substrate ( PqqA ) in the presence of the Radical SAM enzyme ( PqqE ) and its peptide chaperone ( PqqD )

J. Klinman, A. T. Iavarone, J. Latham, 2016 .

Demonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD*♦

J. Klinman, A. T. Iavarone, J. Latham, 2016, The Journal of Biological Chemistry.

PqqD Is a Novel Peptide Chaperone That Forms a Ternary Complex with the Radical S-Adenosylmethionine Protein PqqE in the Pyrroloquinoline Quinone Biosynthetic Pathway*

J. Klinman, A. T. Iavarone, J. Latham, 2015, The Journal of Biological Chemistry.

Pyrroloquinoline quinone biogenesis: demonstration that PqqE from Klebsiella pneumoniae is a radical S-adenosyl-L-methionine enzyme.

J. Klinman, O. Magnusson, Shu-Pao Wu, 2009, Biochemistry.

A Crosslinked Cofactor in Lysyl Oxidase: Redox Function for Amino Acid Side Chains

A L Burlingame, J. Klinman, A. Burlingame, 1996, Science.

A link between protein structure and enzyme catalyzed hydrogen tunneling.

J. Klinman, B. Bahnson, J P Klinman, 1997, Proceedings of the National Academy of Sciences of the United States of America.

The Copper-Enzyme Family of Dopamine β-Monooxygenase and Peptidylglycine α-Hydroxylating Monooxygenase: Resolving the Chemical Pathway for Substrate Hydroxylation*

J. Klinman, 2006, Journal of Biological Chemistry.

Enzyme Catalysis: Beyond Classical Paradigms

J. Klinman, A. Kohen, 1998 .

Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics.

Judith P Klinman, J. Klinman, Michael J Knapp, 2002, European journal of biochemistry.

Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1

M. P. Meyer, J. Klinman, D. Tomchick, 2008, Proceedings of the National Academy of Sciences.

Control of the Position of Oxygen Delivery in Soybean Lipoxygenase-1 by Amino Acid Side Chains within a Gas Migration Channel*

J. Klinman, L. Collazo, 2016, The Journal of Biological Chemistry.

Nature of rate-limiting steps in the soybean lipoxygenase-1 reaction.

J. Klinman, M. Glickman, Michael H. Glickman, 1995, Biochemistry.

Steric control of oxygenation regiochemistry in soybean lipoxygenase-1.

J. Klinman, F. Seebeck, M. J. Knapp, 2001, Journal of the American Chemical Society.

Kinetic studies of oxygen reactivity in soybean lipoxygenase-1.

J. Klinman, M. J. Knapp, 2003, Biochemistry.

How do enzymes activate oxygen without inactivating themselves?

J. Klinman, 2007, Accounts of chemical research.

Temperature-dependent isotope effects in soybean lipoxygenase-1: correlating hydrogen tunneling with protein dynamics.

Judith P Klinman, J. Klinman, K. Rickert, 2002, Journal of the American Chemical Society.

Protein function | Kinetic Isotope Effects

J. Klinman, A. Offenbacher, J. Roth, 2021, Encyclopedia of Biological Chemistry III.

The Soybean Lipoxygenase-Substrate Complex: Correlation between the Properties of Tunneling-Ready States and ENDOR-Detected Structures of Ground States.

J. Klinman, Ajay Sharma, B. Hoffman, 2020, Biochemistry.

Moving Through Barriers in Science and Life.

J. Klinman, 2019, Annual review of biochemistry.

Understanding Biological Hydrogen Transfer Through the Lens of Temperature Dependent Kinetic Isotope Effects.

J. Klinman, A. Offenbacher, 2018, Accounts of chemical research.

Understanding Biological Hydrogen Transfer Through the Lens of Temperature Dependent Kinetic Isotope E ff ects Published as part of the Accounts of Chemical Research special issue “ Hydrogen Atom Transfer ” .

J. Klinman, O. AdamR., enbacher, 2018 .

Hydrostatic Pressure Studies Distinguish Global from Local Protein Motions in C-H Activation by Soybean Lipoxygenase-1.

J. Klinman, Shenshen Hu, Jérôme Cattin-Ortolá, 2016, Angewandte Chemie.

Synthesis of Site-Specifically 13C Labeled Linoleic Acids.

J. Klinman, A. Offenbacher, Hui Zhu, 2016, Tetrahedron letters.

Evolutionary Aspects of Enzyme Dynamics*

J. Klinman, A. Kohen, 2014, The Journal of Biological Chemistry.

The widespread occurrence of enzymatic hydrogen tunneling, andits unique properties, lead to a new physical model for the origins of enzyme catalysis

J. Klinman, 2011 .

Enzyme dynamics: Control of active-site compression.

J. Klinman, 2010, Nature chemistry.

A new model for the origin of kinetic hydrogen isotope effects

J. Klinman, 2010 .

An active-site phenylalanine directs substrate binding and C-H cleavage in the alpha-ketoglutarate-dependent dioxygenase TauD.

J. Klinman, Kevin P. McCusker, 2010, Journal of the American Chemical Society.

Quinoenzymes in biology.

J. Klinman, D. Mu, 1994, Annual review of biochemistry.

Bovine membranous dopamine beta-hydroxylase is not anchored via covalently attached phosphatidylinositol.

J. Klinman, L. Stewart, 1988, The Journal of biological chemistry.

Oxygen Kinetic Isotope Effects in Soluble Methane Monooxygenase*

J. Klinman, M. Merkx, S. Lippard, 2001, The Journal of Biological Chemistry.

Tetrazine Marks the Spot

J. Klinman, R. Row, Jennifer A. Prescher, 2016, ACS central science.

Trihydroxyphenylalanine quinone (TPQ) from copper amine oxidases and lysyl tyrosylquinone (LTQ) from lysyl oxidase.

J. Klinman, J. Dove, 2001, Advances in protein chemistry.

Identification of the quinone cofactor in a lysyl oxidase from Pichia pastoris

J. Klinman, A. Smith, Doreen E. Brown, 1996, FEBS letters.

Identification of topaquinone and its consensus sequence in copper amine oxidases.

J. Klinman, A. Smith, M. Palcic, 1992, Biochemistry.

The nature of O2 activation by the ethylene-forming enzyme 1-aminocyclopropane-1-carboxylic acid oxidase

J. Klinman, Liviu M. Mirica, 2008, Proceedings of the National Academy of Sciences.

Mechanistic investigations of 1-aminocyclopropane 1-carboxylic acid oxidase with alternate cyclic and acyclic substrates.

J. Klinman, J. Thrower, Liviu M. Mirica, 2006, Biochemistry.

A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase.

J. Klinman, A. Burlingame, D. Wemmer, 1990, Science.

Primary structures for a mammalian cellular and serum copper amine oxidase.

J. Klinman, A. Burlingame, K. Medzihradszky, 1994, The Journal of biological chemistry.

The isolation and characterization of active site peptides in lysyl oxidase

J. Klinman, A. Burlingame, K. Medzihradszky, 1997 .

Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway.

J. Klinman, C. Wilmot, J. Latham, 2019, Journal of the American Chemical Society.

Structural analysis of aliphatic versus aromatic substrate specificity in a copper amine oxidase from Hansenula polymorpha.

J. Klinman, C. Wilmot, V. J. Klema, 2013, Biochemistry.

Hydrogen tunneling in the flavoenzyme monoamine oxidase B.

J. Klinman, T. Jonsson, D. Edmondson, 1994, Biochemistry.

Structure of bovine adrenal dopamine beta-monooxygenase, as deduced from cDNA and protein sequencing: evidence that the membrane-bound form of the enzyme is anchored by an uncleaved signal peptide.

J. Klinman, A. Smith, L. Stewart, 1989, Biochemistry.

Primary Hydrogen Isotope Effects

J. Klinman, 1978 .

Temporal and Spatial Resolution of a Protein Quake that Activates Hydrogen Tunneling in Soybean Lipoxygenase

J. Klinman, C. Gee, A. Offenbacher, 2022, bioRxiv.

Pathway for the Stereocontrolled Z and E Production of α,α-Difluorine-Substituted Phenyl Butenoates

J. Klinman, Corinna R. Hess, G. Iacazio, 2006 .

Effects of enzyme glycosylation on the chemical step of catalysis, as probed by hydrogen tunneling and enthalpy of activation

J. Klinman, T. Jonsson, A. Kohen, 1997 .

NMR structure and binding studies of PqqD, a chaperone required in the biosynthesis of the bacterial dehydrogenase cofactor pyrroloquinoline quinone

J. Klinman, J. Latham, Youlin Xia, 2017 .

Distribution and properties of the genes encoding the biosynthesis of the bacterial cofactor, pyrroloquinoline quinone.

K. Sjölander, J. Klinman, Yaoqing Shen, 2012, Biochemistry.

pH dependence of deuterium isotope effects and tritium exchange in the bovine plasma amine oxidase reaction: a role for single-base catalysis in amine oxidation and imine exchange.

J. Klinman, M. Palcic, M. Farnum, 1986, Biochemistry.

Temperature-dependent hydrogen deuterium exchange shows impact of analog binding on adenosine deaminase flexibility but not embedded thermal networks

J. Klinman, A. Iavarone, Shuaihua Gao, 2022, The Journal of biological chemistry.

Identification of Thermal Conduits That Link the Protein-Water Interface to the Active Site Loop and Catalytic Base in Enolase.

J. Klinman, Emily J Thompson, A. Iavarone, 2021, Journal of the American Chemical Society.

A two-component protease in Methylorubrum extorquens with high activity toward the peptide precursor of the redox cofactor pyrroloquinoline quinone

J. Klinman, P. Martel, J. Latham, 2019, The Journal of Biological Chemistry.

Oxygen-18 Isotope Effects as a Probe of Enzymatic Activation of Molecular Oxygen

J. Klinman, J. Klinman, 2005 .

The Catalytic Function of Bovine Lysyl Oxidase in the Absence of Copper*

J. Klinman, Chunlin Tang, 2001, The Journal of Biological Chemistry.

New Quinocofactors in Eukaryotes*

J. Klinman, 1996, The Journal of Biological Chemistry.

Modular behavior of tauD provides insight into the origin of specificity in α-ketoglutarate-dependent nonheme iron oxygenases

J. Klinman, Kevin P. McCusker, 2009, Proceedings of the National Academy of Sciences.

Facile synthesis of 1,1-[2H2]-2-methylaminoethane-1-sulfonic acid as a substrate for taurine α ketoglutarate dioxygenase (TauD)

J. Klinman, Kevin P. McCusker, 2009 .

Structural Properties and Catalytic Implications of the SPASM Domain Iron-Sulfur Clusters in Methylorubrum extorquens PqqE.

J. Klinman, S. Elliott, R. D. Britt, 2020, Journal of the American Chemical Society.

Activation of dopamine beta-monooxygenase by external and internal electron donors in resealed chromaffin granule ghosts.

J. Klinman, N. Ahn, 1987, The Journal of biological chemistry.

J. Klinman, R. Dyer, T. Spiro, 2018, Journal of the American Chemical Society.

Electron Paramagnetic Resonance Spectroscopic Identification of the Fe–S Clusters in the SPASM-Domain Containing Radical SAM Enzyme PqqE

J. Klinman, R. D. Britt, Lizhi Tao, 2020 .

EPR Spectroscopic Identification of the Fe-S Clusters in the SPASM-Domain Containing Radical SAM Enzyme PqqE.

J. Klinman, R. D. Britt, Lizhi Tao, 2019, Biochemistry.

Functional roles of enzyme dynamics in accelerating active site chemistry: Emerging techniques and changing concepts.

J. Klinman, Shuaihua Gao, 2022, Current opinion in structural biology.

Corrigendum: A 21 st century revisionist's view at a turning point in enzymology

J. Klinman, Z. Nagel, 2009 .

New Probes of Oxygen Binding and Activation: Application to Dopamine β-Monooxygenase

J. Klinman, J. Berry, G. Tian, 1992 .

The structure of a biosynthetic intermediate of pyrroloquinoline quinone (PQQ) and elucidation of the final step of PQQ biosynthesis.

J. Klinman, R. Schwarzenbacher, O. Magnusson, 2004, Journal of the American Chemical Society.

Multistep, eight-electron oxidation catalyzed by the cofactorless oxidase, PqqC: identification of chemical intermediates and their dependence on molecular oxygen.

J. Klinman, A. Iavarone, F. Bonnot, 2013, Biochemistry.

High-performance liquid chromatography separation of the (S,S)- and (R,S)-forms of S-adenosyl-L-methionine.

J. Klinman, Jianyu Zhang, 2015, Analytical biochemistry.

Effect of Metal on 2,4,5-Trihydroxyphenylalanine (Topa) Quinone Biogenesis in the Hansenula polymorpha Copper Amine Oxidase*

N. K. Williams, J. Klinman, Danying Cai, 1997, The Journal of Biological Chemistry.

Emerging concepts about the role of protein motion in enzyme catalysis.

J. Klinman, S. Hammes‐Schiffer, 2015, Accounts of chemical research.

Oxygen‐Activating Enzymes, Chemistry of

J. Klinman, Corinna R. Hess, R. Welford, 2008 .

Mechanism of the aconitate isomerase reaction.

J. Klinman, I. A. Rose, 1971, Biochemistry.

Investigation of the pathway for inter-copper electron transfer in peptidylglycine alpha-amidating monooxygenase.

J. Klinman, D. Merkler, G. Wille, 2004, Journal of the American Chemical Society.

Insights into the Proposed Copper–Oxygen Intermediates that Regulate the Mechanism of Reactions Catalyzed by Dopamine β‐Monooxygenase, Peptidylglycine α‐Hydroxylating Monooxygenase, and Tyramine β‐Monooxygenase

J. Klinman, Robert L. Osborne, 2011 .

Computational Study of Tunneling and Coupled Motion in Alcohol Dehydrogenase-Catalyzed Reactions: Implication for Measured Hydrogen and Carbon Isotope Effects

J. Klinman, J. Rucker, 1999 .

Interdomain long-range electron transfer becomes rate-limiting in the Y216A variant of tyramine β-monooxygenase.

J. Klinman, Robert L. Osborne, Hui Zhu, 2013, Biochemistry.

Hydroxylase activity of Met471Cys tyramine beta-monooxygenase.

J. Klinman, Erin E Gray, Corinna R. Hess, 2008, Journal of the American Chemical Society.

Kinetic mechanism and intrinsic isotope effects for the peptidylglycine alpha-amidating enzyme reaction.

J. Klinman, D. Merkler, N. Blackburn, 1998, Biochemistry.

Biogenesis of the peptide-derived redox cofactor pyrroloquinoline quinone.

J. Klinman, Wen Zhu, 2020, Current opinion in chemical biology.

Biogenesis of the peptide-derived redox cofactor PQQ

J. Klinman, W. Zhu, Wen Zhu, 2020 .

Role of internal thermodynamics in determining hydrogen tunneling in enzyme-catalyzed hydrogen transfer reactions.

J. Klinman, T. Jonsson, Y. Cha, 1992, Biochemistry.

The role of copper in topa quinone biogenesis and catalysis, as probed by azide inhibition of a copper amine oxidase from yeast.

J. Klinman, B. Schwartz, A. K. Olgin, 2001, Biochemistry.

How many ways to craft a cofactor?

J. Klinman, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Mechanisms Whereby Mononuclear Copper Proteins Functionalize Organic Substrates.

J. Klinman, 1996, Chemical reviews.

Correlation of copper valency with product formation in single turnovers of dopamine beta-monooxygenase.

J. Klinman, J P Klinman, M C Brenner, 1989, Biochemistry.

Structural Snapshots from the Oxidative Half-reaction of a Copper Amine Oxidase

J. Klinman, C. Wilmot, B. J. Johnson, 2013, The Journal of Biological Chemistry.

Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha.

J. Klinman, C. Wilmot, B. J. Johnson, 2010, Biochemistry.

Partial conversion of Hansenula polymorpha amine oxidase into a "plant" amine oxidase: implications for copper chemistry and mechanism.

J. Klinman, R. Welford, Liviu M. Mirica, 2007, Biochemistry.

Stereochemistry and kinetic isotope effects in the bovine plasma amine oxidase catalyzed oxidation of dopamine.

J. Klinman, R. Marković, M. C. Summers, 1979, Biochemistry.

Evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase. Implications for the reactive oxygen species.

J. Klinman, K. Ahn, J. P. Evans, 2003, The Journal of biological chemistry.

Hydrogen Tunneling in Peptidylglycine α-Hydroxylating Monooxygenase

J. Klinman, M. J. Knapp, N. Blackburn, 2002 .

Dopamine beta-hydroxylase of adrenal chromaffin granules: structure and function.

J. Klinman, J P Klinman, L C Stewart, 1988, Annual review of biochemistry.

Rapid freeze- and chemical-quench studies of dopamine beta-monooxygenase: comparison of pre-steady-state and steady-state parameters.

C. J. Murray, J. Klinman, M. Brenner, 1989, Biochemistry.

Characterization of alternate reductant binding and electron transfer in the dopamine beta-monooxygenase reaction.

J. Klinman, L. Stewart, 1987, Biochemistry.

Evidence for two copper atoms/subunit in dopamine beta-monooxygenase catalysis.

J. Klinman, D. Edmondson, J P Klinman, 1984, The Journal of biological chemistry.

Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.

J. Klinman, Florence Bonnot, 2014, Chemical reviews.

Synthesis and characterization of model compounds of the lysine tyrosyl quinone cofactor of lysyl oxidase.

J. Klinman, M. Mure, S. Wang, 2003, Journal of the American Chemical Society.

Catalytic mechanism of the topa quinone containing copper amine oxidases.

J. Klinman, M. Mure, S. A. Mills, 2002, Biochemistry.

An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha.

J. Klinman, J. Sanders-Loehr, J. Plastino, 1999, Biochemistry.

Model Studies of Topaquinone-Dependent Amine Oxidases. 2. Characterization of Reaction Intermediates and Mechanism

J. Klinman, M. Mure, 1995 .

Model Studies of Topaquinone-Dependent Amine Oxidases. 1. Oxidation of Benzylamine by Topaquinone Analogs

J. Klinman, M. Mure, 1995 .

Synthesis and spectroscopic characterization of model compounds for the active site cofactor in copper amine oxidases

J. Klinman, M. Mure, 1993 .

Spectroscopic detection of chemical intermediates in the reaction of para-substituted benzylamines with bovine serum amine oxidase.

J. Klinman, P. Brzovic, C. Hartmann, 1993, Biochemistry.

Synthesis of linoleic acids combinatorially-labeled at the vinylic positions as substrates for lipoxygenases.

M. P. Meyer, J. Klinman, 2008, Tetrahedron letters.

Exponential relationships among multiple hydrogen isotope effects as probes of hydrogen tunneling

J. Klinman, K. L. Grant, 1992 .

Discrimination between 16O and 18O in oxygen binding to the reversible oxygen carriers hemoglobin, myoglobin, hemerythrin, and hemocyanin: a new probe for oxygen binding and reductive activation by proteins

J. Klinman, G. Tian, 1993 .

Oxygen-18 kinetic isotope effects in the dopamine beta-monooxygenase reaction: evidence for a new chemical mechanism in non-heme metallomonooxygenases.

J. Klinman, J. Berry, G. Tian, 1994, Biochemistry.

Isotope effects and structure-reactivity correlations in the yeast alcohol dehydrogenase reaction. A study of the enzyme-catalyzed oxidation of aromatic alcohols.

J. Klinman, 1976, Biochemistry.

Transition-state structure in the yeast alcohol dehydrogenase reaction: the magnitude of solvent and alpha-secondary hydrogen isotope effects.

J. Klinman, K. Welsh, D. J. Creighton, 1980, Biochemistry.

Exploring Molecular Oxygen Pathways in Hansenula polymorpha Copper-containing Amine Oxidase*

Klaus Schulten, Judith P Klinman, Arwen R Pearson, 2007, Journal of Biological Chemistry.

Eukaryotic Copper Amine Oxidases

J. Klinman, D. L. Wertz, Diana L. Wertz, 2006 .

Whence topa? Models for the biogenesis of topa quinone in copper amine oxidases

N. K. Williams, J. Klinman, 2000 .

Copper amine oxidase from Hansenula polymorpha: the crystal structure determined at 2.4 A resolution reveals the active conformation.

F. S. Mathews, J. Klinman, R. Li, 1998, Structure.

Surprises among quinoproteins

J. Klinman, 1991 .

Evidence that both protium and deuterium undergo significant tunneling in the reaction catalyzed by bovine serum amine oxidase.

J. Klinman, J P Klinman, K. L. Grant, 1989, Biochemistry.

Mechanism of post-translational quinone formation in copper amine oxidases and its relationship to the catalytic turnover.

J. Klinman, J. DuBois, 2005, Archives of biochemistry and biophysics.

The multi-functional topa-quinone copper amine oxidases.

Judith P Klinman, J. Klinman, 2003, Biochimica et biophysica acta.

Mechanistic comparison of the cobalt-substituted and wild-type copper amine oxidase from Hansenula polymorpha.

J. Klinman, Y. Goto, J. Plastino, 2002, Biochemistry.

An investigation of bovine serum amine oxidase active site stoichiometry: evidence for an aminotransferase mechanism involving two carbonyl cofactors per enzyme dimer.

J. Klinman, S. Janes, 1991, Biochemistry.

Structure-function studies of substrate oxidation by bovine serum amine oxidase: relationship to cofactor structure and mechanism.

J. Klinman, C. Hartmann, 1991, Biochemistry.

The organic functional group in copper-containing amine oxidases. Resonance Raman spectra are consistent with the presence of topa quinone (6-hydroxydopa quinone) in the active site.

J. Klinman, D. Dooley, D. Mu, 1991, The Journal of biological chemistry.

Characterization of the Native Lysine Tyrosylquinone Cofactor in Lysyl Oxidase by Raman Spectroscopy*

J. Klinman, N. Nakamura, J. Sanders-Loehr, 1997, The Journal of Biological Chemistry.

Reductive trapping of substrate to bovine plasma amine oxidase.

J. Klinman, C. Hartmann, 1987, The Journal of biological chemistry.

Probing the mechanism of proton coupled electron transfer to dioxygen: the oxidative half-reaction of bovine serum amine oxidase.

J. Klinman, Q. Su, 1998, Biochemistry.

Isotopic probes yield microscopic constants: separation of binding energy from catalytic efficiency in the bovine plasma amine oxidase reaction.

J. Klinman, M. Palcic, 1983, Biochemistry.

FIRST REACTIONS

J. Klinman, 2021, Soviet-American Relations, 1917-1920, Volume I.

The copper centers of tyramine β-monooxygenase and its catalytic-site methionine variants: an X-ray absorption study

J. Klinman, Corinna R. Hess, N. Blackburn, 2010, JBIC Journal of Biological Inorganic Chemistry.

Dopamine beta-hydroxylase: activity and inhibition in the presence of beta-substituted phenethylamines.

J. Klinman, M. Krueger, 1982, Biochemistry.

Deduction of kinetic mechanism in multisubstrate enzyme reactions from tritium isotope effects. Application to dopamine beta-hydroxylase.

J. Klinman, J. Voet, H. Humphries, 1980, The Journal of biological chemistry.

The mechanism of enzyme-catalyzed reduced nicotinamide adenine dinucleotide-dependent reductions. Substituent and isotope effects in the yeast alcohol dehydrogenase reaction.

J. Klinman, 1972, The Journal of biological chemistry.

Oxygen-18 Kinetic Isotope Effects of Nonheme Iron Enzymes HEPD and MPnS Support Iron(III) Superoxide as the Hydrogen Abstraction Species

J. Klinman, W. A. van der Donk, Hui Zhu, 2015, Journal of the American Chemical Society.

Probes of mechanism and transition-state structure in the alcohol dehydrogenase reaction.

J. Klinman, J P Klinman, 1981, CRC critical reviews in biochemistry.

The interaction of an epoxide with yeast alcohol dehydrogenase: evidence for binding and the modification of two active site cysteines by styrene oxide.

J. Klinman, 1975, Biochemistry.

Epoxide inhibition of alcohol dehydrogenases. Identification of modified cysteines in yeast alcohol dehydrogenase and demonstration of reversible and irreversible inhibition of liver alcohol dehydrogenase by styrene oxide.

J. Klinman, K. Welsh, R. Hogue-Angeletti, 1977, Biochemistry.

Acid-base catalysis in the yeast alcohol dehydrogenase reaction.

J. Klinman, 1975, The Journal of biological chemistry.

Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments

Jie Zheng, Albert J R Heck, Christoph Borchers, 2019, Nature Methods.

Solvent and Temperature Probes of the Long-Range Electron-Transfer Step in Tyramine β-Monooxygenase: Demonstration of a Long-Range Proton-Coupled Electron-Transfer Mechanism

J. Klinman, Hui Zhu, M. Sommerhalter, 2015, Journal of the American Chemical Society.

Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase.

J. Klinman, D. Cai, 1994, The Journal of biological chemistry.

Copper amine oxidase: heterologous expression, purification, and characterization of an active enzyme in Saccharomyces cerevisiae.

J. Klinman, D. Cai, 1994, Biochemistry.

Hydrogen tunneling in biology.

J. Klinman, A. Kohen, Amnon Kohen, 1999, Chemistry & biology.

Stereochemical probes of bovine plasma amine oxidase: evidence for mirror image processing and a syn abstraction of hydrogens from C-1 and C-2 of dopamine.

J. Klinman, M. Farnum, 1986, Biochemistry.

Stereochemistry of oxidation of benzylamine by the amine oxidase from beef plasma

J. Klinman, J. Staunton, A. Battersby, 1979, FEBS Letters.

Stereochemistry and kinetic isotope effects in the decarboxylation of S-adenosylmethionine catalyzed by the pyruvyl enzyme, S-adenosylmethionine decarboxylase.

R. R. Allen, J. Klinman, 1981, The Journal of biological chemistry.

Mechanism-based inactivation of dopamine beta-monooxygenase by beta-chlorophenethylamine.

J. Klinman, J. Mangold, 1984, The Journal of biological chemistry.

Mechanism of modulation of dopamine beta-monooxygenase by pH and fumarate as deduced from initial rate and primary deuterium isotope effect studies.

J. Klinman, N. Ahn, 1983, Biochemistry.

The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with CuI and CoII.

J. Klinman, C. Wilmot, B. J. Johnson, 2012, Acta crystallographica. Section F, Structural biology and crystallization communications.

Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.

J. Klinman, S. Datta, J. DuBois, 2010, Biochemistry.

Investigation of cu(I)-dependent 2,4,5-Trihydroxyphenylalanine Quinone Biogenesis in Hansenula polymorpha Amine Oxidase*

J. Klinman, N. Samuels, 2006, Journal of Biological Chemistry.

Methods for characterizing TPQ-containing proteins.

J. Klinman, J. DuBois, 2004, Methods in enzymology.

Quinocofactors in Copper Amine Oxidases and Lysyl Oxidase

J. Klinman, D. Cai, S. Wang, 1996 .

Limited proteolysis of Hansenula polymorpha yeast amine oxidase: isolation of a C‐terminal fragment containing both a copper and quino‐cofactor

J. Klinman, J. Plastino, 1995, FEBS letters.

Status of the cofactor identity in copper oxidative enzymes

B Mondovi, J. Klinman, P. Knowles, 1991, FEBS letters.

Mechanisms of biosynthesis of protein-derived redox cofactors.

J. Klinman, B. Schwartz, 2001, Vitamins and hormones.

SOLVENT ISOTOPE EFFECTS IN THE YEAST ALCOHOL DEHYDROGENASE REACTION

J. Klinman, K. Welsh, D. J. Creighton, 1977 .

The zinc content of yeast alcohol dehydrogenase.

J. Klinman, K. Welsh, 1976, Biochemical and biophysical research communications.

Calculation of substrate dissociation constants from steady-state isotope effects in enzyme-catalyzed reactions

J. Klinman, R. Matthews, 1985 .

Crystal structure and amide H/D exchange of binary complexes of alcohol dehydrogenase from Bacillus stearothermophilus: insight into thermostability and cofactor binding.

J. Klinman, B. Bahnson, G. Prehna, 2004, Biochemistry.

Stereochemistry of the interconversions of citrate and acetate catalyzed by citrate synthase, adenosine triphosphate citrate lyase, and citrate lyase.

J. Klinman, I. A. Rose, 1971, Biochemistry.

Purification and kinetic properties of aconitate isomerase from Pseudomonas putida.

J. Klinman, I. A. Rose, 1971, Biochemistry.

Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase.

J. Klinman, J. Thrower, R. Blalock, 2001, Biochemistry.

Mechanism of inhibition of dopamine beta-monooxygenase by quinol and phenol derivatives, as determined by solvent and substrate deuterium isotope effects.

J. Klinman, S. C. Kim, 1991, Biochemistry.

Hydrogen–deuterium exchange reveals long-range dynamical allostery in soybean lipoxygenase

J. Klinman, A. Offenbacher, A. Iavarone, 2017, The Journal of Biological Chemistry.

Structure Function Studies of Dopamine β-Hydroxylase

J. Klinman, L. Stewart, J. Taljanidisz, 1990 .

De novo design and utilization of photolabile caged substrates as probes of hydrogen tunneling with horse liver alcohol dehydrogenase at sub-zero temperatures: a cautionary note.

J. Klinman, S. Tsai, 2003, Bioorganic chemistry.

Hydrogen-Transfer Reactions

J. Klinman, R. Schowen, J. Hynes, 2006 .

Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone.

R. Liddington, J. Klinman, R. Schwarzenbacher, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Picosecond-Resolved Fluorescent Probes at Functionally Distinct Tryptophans within a Thermophilic Alcohol Dehydrogenase: Relationship of Temperature-Dependent Changes in Fluorescence to Catalysis

J. Klinman, Corey W Meadows, Ryan Ou, 2014, The journal of physical chemistry. B.

Update 1 of: Tunneling and dynamics in enzymatic hydride transfer.

J. Klinman, Z. Nagel, 2010, Chemical reviews.

Evidence for increased local flexibility in psychrophilic alcohol dehydrogenase relative to its thermophilic homologue.

J. Klinman, K. Resing, N. Ahn, 2004, Biochemistry.

Implication for Functions of the Ectopic Adipocyte Copper Amine Oxidase (AOC3) from Purified Enzyme and Cell-Based Kinetic Studies

J. Klinman, Sam H. Shen, D. L. Wertz, 2012, PloS one.

Hydrogen Tunneling in a Prokaryotic Lipoxygenase

J. Klinman, C. Carr, C. A. M. Carr, 2014, Biochemistry.

X-ray and EPR Characterization of the Auxiliary Fe-S Clusters in the Radical SAM Enzyme PqqE.

J. Klinman, S. Almo, J. Bonanno, 2018, Biochemistry.

Hydrogen-Deuterium Exchange within Adenosine Deaminase, a TIM Barrel Hydrolase, Identifies Networks for Thermal Activation of Catalysis.

J. Klinman, Emily J Thompson, A. Iavarone, 2020, Journal of the American Chemical Society.

Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catechol O-methyltransferase reaction

J. Klinman, N. Ahn, Jeremy L. Balsbaugh, 2020, Proceedings of the National Academy of Sciences.

Reductive trapping of substrate to methylamine oxidase from Arthrobacter P1

J. Klinman, C. Hartmann, Judith P. Klinman, 1990, FEBS letters.

Cloning and characterization of histamine dehydrogenase from Nocardioides simplex.

J. Klinman, M. Mure, J. Limburg, 2005, Archives of biochemistry and biophysics.

Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases.

J. Klinman, A. Smith, Doreen E. Brown, 1992, The Journal of biological chemistry.

1H, 13C, and 15N resonance assignments and secondary structure information for Methylobacterium extorquens PqqD and the complex of PqqD with PqqA

J. Klinman, C. Wilmot, J. Latham, 2016, Biomolecular NMR Assignments.

1H, 13C, and 15N resonance assignments and secondary structure information for Methylobacterium extorquens PqqD and the complex of PqqD with PqqA

J. Klinman, C. Wilmot, J. Latham, 2016, Biomolecular NMR assignments.

Isolation of 2,4,5-trihydroxyphenylalanine quinone (topa quinone) from copper amine oxidases.

J. Klinman, S. Janes, 1995, Methods in enzymology.

Pyrroloquinoline quinone: a new redox cofactor in eukaryotic enzymes.

J. Klinman, C. Hartmann, 1988, BioFactors.

Methods for Expression, Purification, and Characterization of PqqE, a Radical SAM Enzyme in the PQQ Biosynthetic Pathway.

J. Klinman, A. M. Martins, Wen Zhu, 2018, Methods in enzymology.

Nuclear Magnetic Resonance Structure and Binding Studies of PqqD, a Chaperone Required in the Biosynthesis of the Bacterial Dehydrogenase Cofactor Pyrroloquinoline Quinone.

J. Klinman, C. Wilmot, J. Latham, 2017, Biochemistry.

Steady-state kinetic investigation of cytochrome P450cam: interaction with redox partners and reaction with molecular oxygen.

J. Klinman, P. Ortiz de Montellano, Matthew M Purdy, 2004, Biochemistry.

How Large Should the QM Region Be in QM/MM Calculations? The Case of Catechol O-Methyltransferase

Heather J. Kulik, Todd J. Martínez, J. Klinman, 2015, The journal of physical chemistry. B.

The power of integrating kinetic isotope effects into the formalism of the Michaelis–Menten equation

J. Klinman, 2014, The FEBS journal.

Detecting and Characterizing the Kinetic Activation of Thermal Networks in Proteins: Thermal Transfer from a Distal, Solvent-Exposed Loop to the Active Site in Soybean Lipoxygenase.

J. Klinman, A. Offenbacher, J. P. T. Zaragoza, 2019, The journal of physical chemistry. B.

Oxygen isotope effects on electron transfer to O2 probed using chemically modified flavins bound to glucose oxidase.

J. Klinman, W. McIntire, D. Edmondson, 2004, Journal of the American Chemical Society.

A 21st century revisionist's view at a turning point in enzymology.

Judith P Klinman, J. Klinman, Z. Nagel, 2009, Nature chemical biology.

Dynamics in Enzyme Catalysis

Sharon Hammes-Schiffer, J. Klinman, Judith P. Klinman, 2013 .

Dynamically Achieved Active Site Precision in Enzyme Catalysis

J. Klinman, Judith P. Klinman, 2014, Accounts of chemical research.

Temperature dependence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiency

J. Klinman, K. Resing, N. Ahn, 2010, Proceedings of the National Academy of Sciences.

Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase

Amnon Kohen, J. Klinman, A. Kohen, 1999, Nature.

Hydrogen tunneling links protein dynamics to enzyme catalysis.

Judith P Klinman, Amnon Kohen, J. Klinman, 2013, Annual review of biochemistry.

Linking protein structure and dynamics to catalysis: the role of hydrogen tunnelling

Judith P Klinman, J. Klinman, 2006, Philosophical Transactions of the Royal Society B: Biological Sciences.

Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.

J. Klinman, B. Bahnson, T. Colby, 1998, Biochemistry.

Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues.

J. Klinman, D. Wemmer, Seok-Yong Lee, 2005, Biochemistry.

Effects of protein glycosylation on catalysis: changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction.

J. Klinman, T. Jonsson, A. Kohen, 1997, Biochemistry.

Origins of Enzyme Catalysis: Experimental Findings for C-H Activation, New Models, and Their Relevance to Prevailing Theoretical Constructs.

J. Klinman, Shenshen Hu, A. Offenbacher, 2017, Journal of the American Chemical Society.

Lipoxygenase reaction mechanism: demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover.

J. Klinman, M. Glickman, 1996, Biochemistry.

Comparative Hydrogen–Deuterium Exchange for a Mesophilic vs Thermophilic Dihydrofolate Reductase at 25 °C: Identification of a Single Active Site Region with Enhanced Flexibility in the Mesophilic Protein

J. Klinman, K. Resing, N. Ahn, 2011, Biochemistry.

Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ) biosynthetic pathway links PqqD to the radical SAM superfamily.

J. Klinman, R. D. Britt, S. Stoll, 2010, Chemical communications.

Topaquinone-dependent amine oxidases: identification of reaction intermediates by Raman spectroscopy.

J. Klinman, N. Nakamura, K. Tanizawa, 1997, Biochemistry.

Dynamical activation of function in metalloenzymes

J. Klinman, 2022, FEBS letters.

Active site hydrophobic residues impact hydrogen tunneling differently in a thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures.

J. Klinman, B. Bahnson, Z. Nagel, 2012, Biochemistry.

Impaired protein conformational landscapes as revealed in anomalous Arrhenius prefactors

J. Klinman, B. Bahnson, Z. Nagel, 2011, Proceedings of the National Academy of Sciences.

Kinetic Detection of Orthogonal Protein and Chemical Coordinates in Enzyme Catalysis: Double Mutants of Soybean Lipoxygenase

J. Klinman, Sudhir C. Sharma, Judith P. Klinman, 2015, Biochemistry.

Picosecond-Resolved Fluorescence Studies of Substrate and Cofactor-Binding Domain Mutants in a Thermophilic Alcohol Dehydrogenase Uncover an Extended Network of Communication

J. Klinman, J. Tsang, Corey W Meadows, 2014, Journal of the American Chemical Society.

Importance of protein dynamics during enzymatic C-H bond cleavage catalysis.

J. Klinman, 2013, Biochemistry.

Enzyme Catalysis: Beyond Classical Paradigms†

Amnon Kohen, J. Klinman, A. Kohen, 1998 .

Hydrogen–Deuterium Exchange of Lipoxygenase Uncovers a Relationship between Distal, Solvent Exposed Protein Motions and the Thermal Activation Barrier for Catalytic Proton-Coupled Electron Tunneling

J. Klinman, Alexander D. Scouras, E. Poss, 2017, ACS central science.

Enhanced Rigidification within a Double Mutant of Soybean Lipoxygenase Provides Experimental Support for Vibronically Nonadiabatic Proton-Coupled Electron Transfer Models

J. Klinman, A. Soudackov, Shenshen Hu, 2017, ACS catalysis.

Extremely Elevated Room-Temperature Kinetic Isotope Effects Quantify the Critical Role of Barrier Width in Enzymatic C–H Activation

Sharon Hammes-Schiffer, Tom Alber, J. Klinman, 2014, Journal of the American Chemical Society.

Thermal-activated protein mobility and its correlation with catalysis in thermophilic alcohol dehydrogenase.

J. Klinman, K. Resing, N. Ahn, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Experimental Evidence for Extensive Tunneling of Hydrogen in the Lipoxygenase Reaction: Implications for Enzyme Catalysis

J. Klinman, T. Jonsson, M. Glickman, 1996 .

13C ENDOR Spectroscopy of Lipoxygenase–Substrate Complexes Reveals the Structural Basis for C–H Activation by Tunneling

J. Klinman, B. Hoffman, Tao Yu, 2017, Journal of the American Chemical Society.

Identification of a Long-range Protein Network That Modulates Active Site Dynamics in Extremophilic Alcohol Dehydrogenases*

J. Klinman, Z. Nagel, S. Cun, 2013, The Journal of Biological Chemistry.

Structural bases of hydrogen tunneling in enzymes: progress and puzzles.

J. Klinman, Zhao-Xun Liang, 2004, Current opinion in structural biology.

Catalysis of electron transfer during activation of O2 by the flavoprotein glucose oxidase

J. Klinman, J. Roth, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Convergent Mechanistic Features between the Structurally Diverse N- and O-Methyltransferases: Glycine N-Methyltransferase and Catechol O-Methyltransferase

J. Klinman, Jianyu Zhang, 2016, Journal of the American Chemical Society.

Environmentally coupled hydrogen tunneling

J. Klinman, Judith P. Klinman, Michael J. Knapp, 2002 .

An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling.

J. Klinman, 2009, Chemical physics letters.

The role of tunneling in enzyme catalysis of C-H activation.

Judith P Klinman, J. Klinman, 2006, Biochimica et biophysica acta.

Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis.

J. Klinman, D. H. Park, B. Bahnson, 1993, Biochemistry.

[14] Hydrogen tunneling in enzyme catalysis

J. Klinman, B. Bahnson, 1995 .

Hydrogen tunneling in enzyme catalysis.

J. Klinman, B. Bahnson, 1995, Methods in enzymology.

Impact of protein flexibility on hydride-transfer parameters in thermophilic and psychrophilic alcohol dehydrogenases.

J. Klinman, Zhao-Xun Liang, V. Bouriotis, 2004, Journal of the American Chemical Society.

Redox-active amino acids in biology

J. Klinman, 1995 .

Protein Flexibility Correlates with Degree of Hydrogen Tunneling in Thermophilic and Mesophilic Alcohol Dehydrogenases

J. Klinman, Amnon Kohen† and, 2000 .

Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida

J. Klinman, C. Wilmot, J. Latham, 2017, JBIC Journal of Biological Inorganic Chemistry.

Evidence That Dioxygen and Substrate Activation Are Tightly Coupled in Dopamine β-Monooxygenase

J. Klinman, K. Ahn, J. P. Evans, 2003, Journal of Biological Chemistry.

Hydrogen atom transfers in B 12 Enzymes by R. Banerjee, D. G. Truhlar, A. Dybala-Defratyka, P. Paneth, in Biological Aspects of Hydrogen Transfer,

J. Klinman, R. Schowen, 2005 .

18O kinetic isotope effects in non-heme iron enzymes: probing the nature of Fe/O2 intermediates.

J. Klinman, Hung‐wen Liu, Liviu M. Mirica, 2008, Journal of the American Chemical Society.

Nature of oxygen activation in glucose oxidase from Aspergillus niger: the importance of electrostatic stabilization in superoxide formation.

J. Klinman, Q. Su, 1999, Biochemistry.

Enzymatic methyl transfer: role of an active site residue in generating active site compaction that correlates with catalytic efficiency.

J. Klinman, Judith P. Klinman, Jianyu Zhang, 2011, Journal of the American Chemical Society.

Mechanism of the Insect Enzyme, Tyramine β-Monooxygenase, Reveals Differences from the Mammalian Enzyme, Dopamine β-Monooxygenase*

J. Klinman, Corinna R. Hess, Michele M. McGuirl, 2008, Journal of Biological Chemistry.

Mechanism of the insect enzyme, tyramine beta-monooxygenase, reveals differences from the mammalian enzyme, dopamine beta-monooxygenase.

J. Klinman, Corinna R. Hess, Michele M. McGuirl, 2008, The Journal of biological chemistry.

The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase: a kinetic study of the H172A mutant.

J. Klinman, N. Blackburn, J. P. Evans, 2006, Biochemistry.

[8] Cloning of mammalian topa quinone-containing enzymes

J. Klinman, D. Mu, 1995 .

esized and post-translationally modi fi ed peptide natural products : overview and recommendations for a universal nomenclature

P. G. Arnison, M. Bibb, M. Fischbach, 2012 .

Investigation of spectroscopic intermediates during copper-binding and TPQ formation in wild-type and active-site mutants of a copper-containing amine oxidase from yeast.

N. K. Williams, J. Klinman, J. Dove, 2000, Biochemistry.

Kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast.

J. Klinman, J. Dove, B. Schwartz, 2000, Biochemistry.

Oxygen-18 kinetic isotope effect studies of the tyrosine hydroxylase reaction: Evidence of rate limiting oxygen activation

J. Klinman, G. Tian, W. A. Francisco, 1998 .

Life as aerobes: are there simple rules for activation of dioxygen by enzymes?

J. Klinman, 2000, JBIC Journal of Biological Inorganic Chemistry.

Comparative kinetic isotope effects on first- and second-order rate constants of soybean lipoxygenase variants uncover a substrate-binding network

J. Klinman, Shenshen Hu, A. Offenbacher, 2019, The Journal of Biological Chemistry.

Rates of oxygen and hydrogen exchange as indicators of TPQ cofactor orientation in amine oxidases.

J. Klinman, N. Nakamura, D. Dooley, 2002, Biochemistry.

Nuclear Tunneling in the Condensed Phase: Hydrogen Transfer in Enzyme Reactions

M. P. Meyer, J. Klinman, M. J. Knapp, 2007 .

Modeling temperature dependent kinetic isotope effects for hydrogen transfer in a series of soybean lipoxygenase mutants: The effect of anharmonicity upon transfer distance.

M. P. Meyer, J. Klinman, 2005, Chemical physics.

Comparison of rates and kinetic isotope effects using PEG-modified variants and glycoforms of glucose oxidase: the relationship of modification of the protein envelope to C-H activation and tunneling.

J. Klinman, S. Seymour, 2002, Biochemistry.

Probes of hydrogen tunneling with horse liver alcohol dehydrogenase at subzero temperatures.

J. Klinman, S. Tsai, 2001, Biochemistry.

Crystal structures reveal metal-binding plasticity at the metallo-β-lactamase active site of PqqB from Pseudomonas putida

J. Klinman, C. Wilmot, J. Latham, 2017, JBIC Journal of Biological Inorganic Chemistry.

Galactose oxidase as a model for reactivity at a copper superoxide center.

Judith P Klinman, J. Klinman, Liviu M. Mirica, 2009, Journal of the American Chemical Society.

The copper-enzyme family of dopamine beta-monooxygenase and peptidylglycine alpha-hydroxylating monooxygenase: resolving the chemical pathway for substrate hydroxylation.

J. Klinman, 2006, The Journal of biological chemistry.

Hydrogen tunneling in peptidylglycine alpha-hydroxylating monooxygenase.

J. Klinman, M. J. Knapp, N. Blackburn, 2002, Journal of the American Chemical Society.

Structural Analysis of Substrate Specificity in a Copper Amine Oxidase from Hansenula polymorpha

J. Klinman, C. Wilmot, V. J. Klema, 2012 .

Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy.

J. Klinman, N. Nakamura, J. Sanders-Loehr, 1995, Biochemistry.

Role of copper and catalytic mechanism in the copper monooxygenase, dopamine beta-hydroxylase (D beta H).

J. Klinman, M. Brenner, 1988, Progress in clinical and biological research.

Experimental evidence for hydrogen tunneling when the isotopic arrhenius prefactor (A(H)/A(D)) is unity.

J. Klinman, Sudhir C. Sharma, 2008, Journal of the American Chemical Society.

Characterization of a protein-generated O₂ binding pocket in PqqC, a cofactorless oxidase catalyzing the final step in PQQ production.

J. Klinman, R. Schwarzenbacher, H. Toyama, 2011, Biochemistry.

Mediation of donor–acceptor distance in an enzymatic methyl transfer reaction

J. Klinman, T. Martínez, H. Kulik, 2015, Proceedings of the National Academy of Sciences.

Inactivation of Met471Cys tyramine β-monooxygenase results from site-specific cysteic acid formation.

J. Klinman, Corinna R. Hess, Robert L. Osborne, 2012, Biochemistry.

Model studies of topa quinone: synthesis and characterization of topa quinone derivatives.

J. Klinman, M. Mure, 1995, Methods in enzymology.

Investigating inner-sphere reorganization via secondary kinetic isotope effects in the C-H cleavage reaction catalyzed by soybean lipoxygenase: tunneling in the substrate backbone as well as the transferred hydrogen.

M. P. Meyer, J. Klinman, 2011, Journal of the American Chemical Society.

Low Barrier Hydrogen Bonds: Getting Close, but Not Sharing...

J. Klinman, 2015, ACS central science.

Quantum mechanical effects in enzyme-catalysed hydrogen transfer reactions.

J. Klinman, 1989, Trends in biochemical sciences.

Isotopic Probes of the Soybean Lipoxygenase-1 Mechanism

J. Klinman, M. Glickman, 1996 .

Oxygen-18 studies to determine the position of bond cleavage of acetyl phosphate in the presence of divalent metal ions.

J. Klinman, D. Samuel, 1971, Biochemistry.

Structural studies of mutant forms of the PQQ‐forming enzyme PqqC in the presence of product and substrate

J. Klinman, R. Schwarzenbacher, H. Toyama, 2010, Proteins.

Temporal and spatial resolution of distal protein motions that activate hydrogen tunneling in soybean lipoxygenase

J. Klinman, C. Gee, A. Offenbacher, 2023, Proceedings of the National Academy of Sciences of the United States of America.

Kinetic parameters for dimeric and tetrameric forms of bovine dopamine [3‐monooxygenase and their relationship to non‐Michaelis‐Menten behavior

J. Klinman, L. Stewart, 1999, FEBS letters.

Cooperativity in the dopamine beta-monooxygenase reaction. Evidence for ascorbate regulation of enzyme activity.

J. Klinman, L. Stewart, 1991, Journal of Biological Chemistry.

Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli.

N. K. Williams, J. Klinman, Z. Chen, 2000, Biochemistry.

Hydrogen tunneling links protein dynamics to enzyme catalysis.

J. Klinman, A. Kohen, 2013, Annual review of biochemistry.

Importance of protein dynamics during enzymatic C-H bond cleavage catalysis.

J. Klinman, 2013, Biochemistry.

Identification of a Long-range Protein Network That Modulates Active Site Dynamics in Extremophilic Alcohol Dehydrogenases*

J. Klinman, Z. Nagel, S. Cun, 2013, Journal of Biological Chemistry.

Mechanism of O2 activation by cytochrome P450cam studied by isotope effects and transient state kinetics.

J. Klinman, Matthew M Purdy, L. S. Koo, 2006, Biochemistry.

Temperature-Jump Fluorescence Provides Evidence for Fully Reversible Microsecond Dynamics in a Thermophilic Alcohol Dehydrogenase

J. Klinman, T. Spiro, B. Kier, 2015, Journal of the American Chemical Society.

The power of integrating kinetic isotope effects into the formalism of the Michaelis–Menten equation

J. Klinman, 2014, The FEBS journal.

Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.

M. Bibb, B. Shen, M. Fischbach, 2013, Natural product reports.

Molecular Life Sciences

J. Klinman, R. Wells, B. Masters, 2018, Springer New York.

Allosteric activation transitions in enzymes and biomolecular motors : insights from atomistic and coarse-grained simulations

J. Klinman, S. Hammes‐Schiffer, 2016 .

Liver alcohol dehydrogenase.

G Pettersson, J. Klinman, G. Pettersson, 1987, CRC critical reviews in biochemistry.

Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ.

J. Klinman, Florence Bonnot, 2014, Chemical reviews.

Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha.

J. Klinman, J. DuBois, 2006, Biochemistry.

PqqD Is a Novel Peptide Chaperone That Forms a Ternary Complex with the Radical S-Adenosylmethionine Protein PqqE in the Pyrroloquinoline Quinone Biosynthetic Pathway*

J. Klinman, J. Latham, Ian Barr, 2015, The Journal of Biological Chemistry.

Pyrroloquinoline quinone biogenesis: characterization of PqqC and its H84N and H84A active site variants.

J. Klinman, R. Schwarzenbacher, O. Magnusson, 2007, Biochemistry.