J. Fee

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Mandelate racemase from Pseudomonas putida. Affinity labeling of the enzyme by D,L-alpha-phenylglycidate in the presence of magnesium ion.

G. L. Kenyon, G. Hegeman, J. Fee, 1974, Biochemistry.

The properties of parsley ferredoxin and its selenium-containing homolog.

J. Fee, G. Palmer, 1971, Biochimica et biophysica acta.

Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levels.

T. B. Powers, W. Stallings, M. Ludwig, 1983, Proceedings of the National Academy of Sciences of the United States of America.

High-potential states of blue and purple copper proteins.

H. Gray, M. Hill, P. Wittung-Stafshede, 1998, Biochimica et biophysica acta.

Electron transfer among the CuA‐, heme b‐ and a 3‐centers of Thermus thermophilus cytochrome ba 3

O. Farver, J. Fee, I. Pecht, 2006, FEBS letters.

Interactions of Cu(B) with Carbon Monoxide in Cytochrome c Oxidase: Origin of the Anomalous Correlation between the Fe-CO and C-O Stretching Frequencies.

D. Rousseau, T. Egawa, J. Fee, 2015, The journal of physical chemistry. B.

X-ray Absorption Studies on the Mixed-Valence and Fully Reduced Forms of the Soluble CuA Domains of Cytochrome c Oxidase

Mary E. Barr, Simon de Vries, William B. Tolman, 1997 .

The oxidation-reduction potentials of parsley ferredoxin and its selenium-containing homolog.

J. Fee, S. Mayhew, G. Palmer, 1971, Biochimica et biophysica acta.

Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus.

H. Gray, J. Richards, J. Fee, 1996, Biochemistry.

Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures.

W. Stallings, D. Touati, M. Ludwig, 1988, The Journal of biological chemistry.

Detection of two histidyl ligands to CuA of cytochrome oxidase by 35-GHz ENDOR. 14,15N and 63,65Cu ENDOR studies of the CuA site in bovine heart cytochrome aa3 and cytochromes caa3 and ba3 from Thermus thermophilus

Ryszard J. Gurbiel, James A. Fee, B. Hoffman, 1993 .

Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus.

W. Stallings, M. Lah, M. Ludwig, 1995, Biochemistry.

First description of a variant of E. coli lacking superoxide dismutase activity yet able to grow efficiently on minimal, oxygenated medium

J. Fee, E. Niederhoffer, C. Naranjo, 1988 .

Isolation of the Escherichia coli iron superoxide dismutase gene: evidence that intracellular superoxide concentration does not regulate oxygen-dependent synthesis of the manganese superoxide dismutase.

T. Baldwin, C. Bull, J. Fee, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Purification and characterization of the Rieske iron-sulfur protein from Thermus thermophilus. Evidence for a [2Fe-2S] cluster having non-cysteine ligands.

D. Hearshen, R. Hille, J. Fee, 1984, The Journal of biological chemistry.

The cytochrome ba3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping

R. Gennis, J. Hemp, J. Fee, 2009, Proceedings of the National Academy of Sciences.

Combined microspectrophotometric and crystallographic examination of chemically reduced and X-ray radiation-reduced forms of cytochrome ba3 oxidase from Thermus thermophilus: structure of the reduced form of the enzyme.

Bin Liu, C. Stout, S. M. Soltis, 2009, Biochemistry.

Superoxide and manganese(III). Reactions of manganese-EDTA and manganese-CyDTA complexes with molecular oxygen. X-ray structure of potassium manganese-EDTA.2 water

L. T. Chan, J. Stein, J. Fackler, 1979 .

Mandelate racemase from Pseudomonas putida. Subunit composition and absolute divalent metal ion requirement.

G. L. Kenyon, G. Hegeman, J. Fee, 1974, Biochemistry.

Sulfhydryl reactivity of human erythrocyte superoxide dismutase. On the origin of the unusual spectral properties of the protein when prepared by a procedure utilizing chloroform and ethanol for the precipitation of hemoglobin.

J. Fee, R. Briggs, 1978, Biochimica et biophysica acta.

Direct evidence for manganese (III) binding to the manganosuperoxide dismutase of Escherichia coli B.

J. Fee, E. Shapiro, T. Moss, 1976, The Journal of biological chemistry.

The oxygen sensitivity of spinach ferredoxin and other iron-sulfur proteins. The formation of protein-bound sulfur-zero.

D. Petering, J. Fee, G. Palmer, 1971, The Journal of biological chemistry.

On the Question of Superoxide Toxicity and the Biological Function of Superoxide Dismutases

J. Fee, 1982 .

Crystallographic studies of Xe and Kr binding within the large internal cavity of cytochrome ba3 from Thermus thermophilus: structural analysis and role of oxygen transport channels in the heme-Cu oxidases.

C David Stout, C. Stout, J. Fee, 2008, Biochemistry.

The rate-limiting step in O(2) reduction by cytochrome ba(3) from Thermus thermophilus.

D. Rousseau, T. Egawa, J. Fee, 2012, Biochimica et biophysica acta.

Catalyzing NO to N2O in the Nitrogen Cycle

J. Fee, P. Moënne‐Loccoz, 2010, Science.

CO impedes superfast O2 binding in ba3 cytochrome oxidase from Thermus thermophilus

T. Soulimane, J. Fee, I. Szundi, 2010, Proceedings of the National Academy of Sciences.

An unexpected outcome of surface engineering an integral membrane protein: improved crystallization of cytochrome ba(3) from Thermus thermophilus.

Bin Liu, C. Stout, J. Fee, 2007, Acta crystallographica. Section F, Structural biology and crystallization communications.

Properties of a copper-containing cytochrome ba3: a second terminal oxidase from the extreme thermophile Thermus thermophilus.

F. Rusnak, J. Fee, E. Münck, 1988, Proceedings of the National Academy of Sciences of the United States of America.

A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus.

C. Stout, J. Fee, Ying Chen, 2005, Acta crystallographica. Section D, Biological crystallography.

Magnetic circular dichroism study of cytochrome ba3 from Thermus thermophilus: spectral contributions from cytochromes b and a3 and nanosecond spectroscopy of CO photodissociation intermediates.

R. A. Goldbeck, D. Kliger, T. Dawes, 1992, Biochemistry.

Comparison of the spin-lattice relaxation properties of the two classes of [2Fe-2S] clusters in proteins.

P. Bertrand, R. Cammack, J. Fee, 1987, Biochimica et biophysica acta.

Quarter field resonance and integer-spin/half-spin interaction in the EPR of Thermus thermophilus ferredoxin. Possible new fingerprints for three iron clusters.

W. Hagen, J. Fee, M. Johnson, 1985, Biochimica et biophysica acta.

Reaction of cyanide with cytochrome ba3 from Thermus thermophilus: spectroscopic characterization of the Fe(II)a3-CN.Cu(II)B-CN complex suggests four 14N atoms are coordinated to CuB.

R. Dyer, B. Hoffman, W. Woodruff, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Electron-nuclear double resonance spectroscopy of 15N-enriched phthalate dioxygenase from Pseudomonas cepacia proves that two histidines are coordinated to the [2Fe-2S] Rieske-type clusters.

B. Hoffman, M. Sivaraja, D. Ballou, 1989, Biochemistry.

Respiratory proteins from extremely thermophilic, aerobic bacteria.

M. Mather, J. Fee, D. Kuila, 1986, Biochimica et biophysica acta.

Evidence for N coordination to Fe in the [2Fe-2S] clusters of Thermus Rieske protein and phthalate dioxygenase from Pseudomonas.

B. Hoffman, D. Ballou, W. Mims, 1985, The Journal of biological chemistry.

Electron–nuclear double resonance on copper (II) tetraimidazole

J. Fee, R. Sands, H. V. Camp, 1981 .

Observations on the mechanism of the oxygen/dialuric acid-induced hemolysis of vitamin e-deficient rat red blood cells and the protective roles of catalase and superoxide dismutase.

J. Fee, R. Briggs, R. Bergamini, 1975, Archives of biochemistry and biophysics.

Reduction potentials of Rieske clusters: importance of the coupling between oxidation state and histidine protonation state.

A. Crofts, J. Hirst, L. Eltis, 2003, Biochemistry.

The iron electron-nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida.

H. Beinert, W. Orme-Johnson, J. Fee, 1971, Biochimica et biophysica acta.

Electron and proton transfer in the ba3 oxidase from Thermus thermophilus

R. Gennis, P. Brzezinski, J. Fee, 2008, Journal of bioenergetics and biomembranes.

Antisymmetric exchange in [2Fe-2S]1+ clusters: EPR of the Rieske protein from Thermus thermophilus at pH 14.

J. Hirst, J. Fee, E. L. Bominaar, 2004, Journal of the American Chemical Society.

Breaking and re-forming the disulfide bond at the high-potential, respiratory-type Rieske [2Fe-2S] center of thermus thermophilus: characterization of the sulfhydryl state by protein-film voltammetry.

J. Hirst, J. Fee, Y. Zu, 2002, Biochemistry.

Selenomethionine-substituted Thermus thermophilus cytochrome ba3: characterization of the CuA site by Se and Cu K-EXAFS.

M. Hill, A. Pastuszyn, J. Fee, 1999, Biochemistry.

Electrochemistry of the CuA domain of Thermus thermophilus cytochrome ba3

H. Gray, M. Hill, J. Richards, 1996, JBIC Journal of Biological Inorganic Chemistry.

Active site structure of Rieske-type proteins: electron nuclear double resonance studies of isotopically labeled phthalate dioxygenase from Pseudomonas cepacia and Rieske protein from Rhodobacter capsulatus and molecular modeling studies of a Rieske center.

T. Macke, D. Case, B. Hoffman, 1996, Biochemistry.

Electron-transfer studies with the CuA domain of Thermus thermophilus cytochrome ba3

M. Hill, J. Richards, J. Winkler, 1996 .

Engineered Cupredoxins and Bacterial Cytochrome c Oxidases Have Similar CuA Sites: Evidence from Resonance Raman Spectroscopy

M. Saraste, N. Nakamura, C. Dennison, 1995 .

Resonance Raman studies of Rieske-type proteins.

R. Dyer, D. Ballou, W. Woodruff, 1992, Biochimica et biophysica acta.

Evidence for a redox-linked ionizable group associated with the [2Fe-2S] cluster of Thermus Rieske protein.

J. Fee, D. Kuila, 1986, The Journal of biological chemistry.

Electrochemical and infrared spectroscopic analysis of the interaction of the Cu(A) domain and cytochrome c(552) from Thermus thermophilus.

P. Hellwig, B. Ludwig, J. Fee, 2012, Biochimica et biophysica acta.

Studies on the reconstitution of bovine erythrocyte superoxide dismutase. IV. Preparation and some properties of the enzyme in which Co(II) is substituted for Zn(II).

J. Fee, 1973, The Journal of biological chemistry.

Studies of the ferredoxin from Thermus thermophilus.

R. Hille, M. Ludwig, J. Fee, 1983, The Journal of biological chemistry.

Characterization of an orthorhombic crystal form of iron-containing superoxide dismutase from Escherichia coli B.

T. B. Powers, M. Ludwig, J. Fee, 1978, Journal of molecular biology.

Spectroscopic characterization of cytochrome ba3, a terminal oxidase from Thermus thermophilus: comparison of the a3/CuB site to that of bovine cytochrome aa3.

R. Dyer, W. Woodruff, J. Fee, 1994, Biochemistry.

Functional role of Thr-312 and Thr-315 in the proton-transfer pathway in ba3 Cytochrome c oxidase from Thermus thermophilus.

R. Gennis, P. Brzezinski, J. Reimann, 2010, Biochemistry.

An infrared study of the binding and photodissociation of carbon monoxide in cytochrome ba3 from Thermus thermophilus.

W. Woodruff, P. Killough, J. Fee, 1989, The Journal of biological chemistry.

Physical and chemical studies on bacterial superoxide dismutases. Purification and some anion binding properties of the iron-containing protein of Escherichia coli B.

J. Fee, T. O. Slykhouse, 1976, The Journal of biological chemistry.

Resonance Raman spectroscopic evidence for a common [3-iron-4-sulfur] structure among proteins containing three-iron centers

R. Czernuszewicz, T. Spiro, Michael K. Johnson, 1983 .

Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence of the fused gene and analysis of the deduced primary structures for subunits I and III of cytochrome caa3.

M. Mather, J. Fee, S. Hensel, 1993, Journal of Biological Chemistry.

Cadmium-113 nuclear magnetic resonance studies of cadmium-substituted derivatives of bovine superoxide dismutase.

J. Fee, P. D. Ellis, D. B. Bailey, 1980, Biochemistry.

Potentiometric titrations and oxidation--reduction potentials of several iron superoxide dismutases.

K. Asada, D. T. Sawyer, J. Fee, 1983, Biochemistry.

The pH Dependence of the Spectral and Anion Binding Properties of Iron Containing Superoxide Dismutase from E. Coli B: An Explanation for the Azide Inhibition of Dismutase Activity*

A. C. Lees, R. Zidovetzki, J. Fee, 1981 .

Mössbauer study of beef heart cytochrome oxidase. Comparative study of the bovine enzyme and cytochrome c1aa3 from Thermus thermophilus.

J. Fee, G. Palmer, E. Münck, 1983, The Journal of biological chemistry.

Additions and Corrections - Catalysis of Superoxide Dismutation by Iron-Ethylenediaminetetraacetic Acid Complexes. Mechanism of the Reaction and Evidence for the Direct Formation of an Iron(III)-Ethyl-enediaminetetraacetic Acid Peroxo Complex from the Reaction of Superoxide with Iron(II) - Ethylened

J. Groves, J. Fee, G. A. McClusky, 1977 .

Isolation and Partial Sequence of the A‐Protein Gene of Thermus thermophilus Cytochrome c1aa3 a

M. Mather, J. Fee, S. Hensel, 1988, Annals of the New York Academy of Sciences.

The interaction of arsenite with xanthine oxidase.

R. Stewart, R. Hille, V. Massey, 1983, The Journal of biological chemistry.

copper proteins systems containing the “Blue” copper center

J. Fee, 1975 .

Studies on the reconstitution of bovine erythrocyte superoxide dismutase. V. Preparation and properties of derivatives in which both zinc and copper sites contain copper.

J. Fee, R. Briggs, 1975, Biochimica et biophysica acta.

Anion binding to bovine erythrocyte superoxide dismutase. Evidence for multiple binding sites with qualitatively different properties.

B. Gaber, J. Fee, 1972, The Journal of biological chemistry.

Observations on the oxidation-reduction properties of bovine erythrocyte superoxide dismutase.

P. Dicorleto, J. Fee, 1973, Biochemistry.

Superoxide dismutase. Examination of the metal binding sites by electron spin echo spectroscopy.

W. Mims, J. Peisach, J. Fee, 1981, The Journal of biological chemistry.

Preliminary report on the electron paramagnetic resonance spectra of single crystals of bovine erythrocyte superoxide dismutase.

J. Fee, R. Lieberman, 1973, Journal of Biological Chemistry.

The Cu_A Center of a Soluble Domain from Thermus Cytochrome ba_3. An NMR Investigation of the Paramagnetic Protein

H. Gray, I. Bertini, C. Luchinat, 1996 .

Evidence for a coordination position available to solute molecules on one of the metals at the active center of reduced bovine superoxide di smutase.

J. Fee, R. Ward, 1976, Biochemical and biophysical research communications.

Studies on the reconstitution of bovine erythrocyte superoxide dismutase. I. The presence of four divalent metal-binding sites on the apo protein which are different from the native sites.

J. Fee, 1973, Biochimica et biophysica acta.

Anaerobic oxidation-reduction titrations of fungal laccase. Evidence for several high potential electron-accepting sites.

J. Fee, R. Malkin, B. Malmström, 1969, The Journal of biological chemistry.

Superoxide dismutase, a study of the electronic properties of the copper and zinc by X-ray absorption spectroscopy.

P. Eisenberger, J. Peisach, W. Blumberg, 1978, Biochemistry.

An examination of the cyanide derivative of bovine superoxide dismutase with electron-nuclear double resonance.

J. Fee, R. Sands, H. L. van Camp, 1982, Biochimica et biophysica acta.

Nuclear magnetic relaxation dispersion in protein solutions. V. Bovine erythrocyte superoxide dismutase.

S. H. Koenig, R. Brown, B. Gaber, 1972, Biochimica et biophysica acta.

The behavior of holo- and apo-forms of bovine superoxide dismutase at low pH.

W. D. Phillips, J. Fee, 1975, Biochimica et biophysica acta.

Studies on the reconstitution of bovine erythrocyte superoxide dismutase. II. Some observations on the nature of catalyzed superoxide anion dismutation as an enzymatic activity.

J. Fee, R. Natter, G. Baker, 1973, Biochimica et biophysica acta.

On the magnetic properties of cobalt substituted bovine superoxide dismutase derivatives.

J. Fee, T. Moss, 1975, Biochemical and biophysical research communications.

Transition metal electron paramagnetic resonance related to proteins.

J. Fee, 1978, Methods in enzymology.

A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B12.

K. Schepler, J. Fee, R. Sands, 1975, Biochimica et biophysica acta.

Kinetic studies of superoxide dismutases: properties of the manganese-containing protein from Thermus thermophilus

C. Bull, J. Fee, E. Niederhoffer, 1991 .

Cytochromecaa3 from the thermophilic bacteriumThermus thermophilus: A member of the heme-copper oxidase superfamily

M. Mather, J. Fee, K. Surerus, 1993, Journal of bioenergetics and biomembranes.

The reduction of fungal laccase at high pH.

J. Fee, B. Malmström, T. Vänngård, 1970, Biochimica et biophysica acta.

The redox potential of fungal laccase.

J. Fee, B. Malmström, 1968, Biochimica et biophysica acta.

The Physical and Theoretical Chemistry of Oxygen

D. Samuel, J. Fee, B. Malmström, 1968 .

Mössbauer study of a bacterial cytochrome oxidase: cytochrome c1aa3 from Thermus thermophilus.

J. Fee, T. Yoshida, W. Dunham, 1982, The Journal of biological chemistry.

The magnetic susceptibility of spinach ferredoxin from 77-250 degrees K: a measurement of the antiferromagnetic coupling between the two iron atoms.

T. Yonetani, T. Iizuka, J. Fee, 1971, Biochimica et biophysica acta.

The mechanism of iron EDTA catalyzed superoxide dismutation

C. Bull, J. Fee, G. McClune, 1983 .

Structure-function relationships in iron and manganese superoxide dismutases.

W. Stallings, M. Ludwig, J. Fee, 1991, Free radical research communications.

Steady-state kinetic studies of superoxide dismutases: properties of the iron containing protein from Escherichia coli

C. Bull, J. Fee, 1985 .

Steric and Electronic Effects in the Hydrolysis of N-Acylimidazoles and N-Acylimidazolium Ions

T. Fife, J. Fee, 1966 .

X-ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase.

J. Penner‐Hahn, M. Ludwig, D. Tierney, 1995, Biochemistry.

Cytochrome Oxidase Genes from Thermus thermophilus

M. Mather, J. Fee, P. Springer, 1991 .

Relationship of Cytochrome caa3 from Thermus thermophilus to Other Heme- and Copper-Containing Terminal Oxidases

M. Mather, J. Fee, P. Springer, 1990 .

A study of the electron paramagnetic resonance properties of single monoclinic crystals of bovine superoxide dismutase.

J. Fee, R. Sands, R. Lieberman, 1982, The Journal of biological chemistry.

Further characterization of human erythrocyte superoxide dismutase.

J. Fee, R. Briggs, 1978, Biochimica et biophysica acta.

Cyanide binding and active site structure in heme-copper oxidases: normal coordinate analysis of iron-cyanide vibrations of a3(2+)CN- complexes of cytochromes ba3 and aa3.

R. Dyer, Y. Kim, W. Woodruff, 1998, Biospectroscopy.

Inhibition of cholesterol side-chain cleavage by 22-azacholesterol.

R. Counsell, J. Fee, S. E. El Masry, 1971, Biochemical pharmacology.

Probing protein‐cofactor interactions in the terminal oxidases by second derivative spectroscopy: Study of bacterial enzymes with cofactor substitutions and heme a model compounds

P. N. Goudreau, M. Ikeda-Saito, R. Copeland, 1994, Protein science : a publication of the Protein Society.

Equilibrium properties of xanthine oxidase containing FAD analogs of varying oxidation-reduction potential.

R. Hille, V. Massey, J. Fee, 1981, The Journal of biological chemistry.

Is superoxide important in oxygen poisoning

James A. Fee, J. Fee, 1982 .

Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerocheate chrysosporium Burds.

J A Fee, M. Tien, T. Kirk, 1986, The Journal of biological chemistry.

Recombinant Cytochrome rC 557 Obtained from Escherichia coli Cells Expressing a TruncatedThermus thermophilus cycA Gene

D. McRee, A. Pastuszyn, J. Fee, 2001, The Journal of Biological Chemistry.

Integrity of thermus thermophilus cytochrome c552 Synthesized by escherichia coli cells expressing the host‐specific cytochrome c maturation genes, ccmABCDEFGH: Biochemical, spectral, and structural characterization of the recombinant protein

M. Hill, D. McRee, J. Fee, 2000, Protein science : a publication of the Protein Society.

Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus

J. Fee, K. Bradley, E. Niederhoffer, 1990, Journal of bacteriology.

Evidence that superoxide dismutase plays a role in protecting red blood cells against peroxidative hemolysis.

J. Fee, H. D. Teitelbaum, 1972, Biochemical and biophysical research communications.

Iron-ethylenediaminetetraacetic acid (EDTA)-catalyzed superoxide dismutation revisited: an explanation of why the dismutase activity of Fe-EDTA cannot be detected in the cytochrome c/Xanthine oxidase assay system.

C. Bull, E. Fielden, P. O'Neill, 1982, Archives of biochemistry and biophysics.

Novel effect of aromatic compounds on the iron-dependent expression of theEscherichia coli K12 manganese superoxide dismutase (sodA) gene

J. Fee, E. Niederhoffer, 2005, Biology of Metals.

Regulation of sod genes in Escherichia coli: relevance to superoxide dismutase function

J. Fee, 1991, Molecular microbiology.

Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence and analysis of the deduced primary structure of subunit IIc of cytochrome caa3.

M. Mather, J. Fee, P. Springer, 1991, The Journal of biological chemistry.

Studies on cytochrome c oxidase activity of the cytochrome c1aa3 complex from Thermus thermophilus.

J. Fee, T. Yoshida, 1984, The Journal of biological chemistry.

Probing site-specific interactions in protein-DNA complexes using heteronuclear NMR spectroscopy and molecular modeling: binding of Cro repressor to OR3.

C. Tung, C. Tung, J. Gatewood, 1998, Journal of biomolecular structure & dynamics.

Cloning and Expression in Escherichia coli of the Cytochrome c 552 Gene from Thermus thermophilus HB8

A. Pastuszyn, J. Fee, D. Sanders, 1998, The Journal of Biological Chemistry.

Application of fast Fourier transforms to EPR spectra of free radicals in solution

H. Grande, J. Fee, L. J. Harding, 1980 .

Observations on the c-type cytochromes of the extreme thermophile, Thermus thermophilus HB8: cytochrome c552 is located in the periplasmic space.

R. Lorence, J. Fee, T. Yoshida, 1981, Biochemical and biophysical research communications.

RESPIRATORY PROTEINS OF SOME EXTREMELY THERMOPHILIC BACTERIA

A. C. Lees, J. Fee, K. Findling, 1978 .

Resonance Raman spectra of extracellular ligninase: evidence for a heme active site similar to those of peroxidases

Mark R. Ondrias, Ming Tien, James A. Fee, 1985 .

Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.

R. Lorence, J. Fee, T. Yoshida, 1980, Proceedings of the National Academy of Sciences of the United States of America.

Evidence for cytochrome oxidase subunit I and a cytochrome c--subunit II fused protein in the cytochrome 'c1aa3' of Thermus thermophilus. How old is cytochrome oxidase?

J. Fee, S. Hensel, G. Buse, 1989, European journal of biochemistry.

Potentiometric study of cytochrome c1aa3 from Thermus thermophilus.

J. Fee, T. Yoshida, 1985, Journal of inorganic biochemistry.

A homologous expression system for obtaining engineered cytochrome ba3 from Thermus thermophilus HB8.

J. Fee, Ying Chen, L. Hunsicker-Wang, 2005, Protein expression and purification.

Cytochrome c Oxidase: A Brief Introduction and Some New Results from High Field Endor Studies of The CuA and CuB Sites

B. Hoffman, J. Fee, W. Antholine, 1993 .

On the development of a well‐defined source of superoxide ion for studies with biological systems

J. Fee, P. Hildenbrand, 1974, FEBS letters.

Steady-state kinetic studies of superoxide dismutases. Saturative behavior of the copper- and zinc-containing protein.

C. Bull, J. Fee, 1986, The Journal of biological chemistry.

Stopped flow spectrophotometric observation of superoxide dismutation in aqueous solution

J. Fee, G. McClune, 1976, FEBS letters.

A Chinese hamster fibroblast mutant defective in thrombin-induced signaling has a low level of phospholipase C-beta 1.

J. Monsey, J. Fee, D. F. Silbert, 1994, The Journal of biological chemistry.

Resonance Raman spectra of the [2Fe-2S] clusters of the Rieske protein from Thermus and phthalate dioxygenase from Pseudomonas

D. Ballou, W. Woodruff, J. Fee, 1987 .

Recombinant Cytochrome rC557 Obtained from Escherichia coli Cells Expressing a Truncated Thermus thermophilus cycA Gene HEME INVERSION IN AN IMPROPERLY MATURED PROTEIN*

D. McRee, A. Pastuszyn, J. Fee, 2001 .

Role of the Conserved Valine 236 in Access of Ligands to the Active Site of Thermus thermophilus ba3 Cytochrome Oxidase.

C. Stout, J. Fee, I. Szundi, 2017, Biochemistry.

Oxidation of deoxy myoglobin by [Fe(CN)6]3-.

J. Fee, C. J. Dunn, R. Rohlfs, 1999, Journal of inorganic biochemistry.

Spectroscopic studies of the seven-iron-containing ferredoxins from Azotobacter vinelandii and Thermus thermophilus.

J. Fee, W. Sweeney, D. E. Bennett, 1987, Biochimica et biophysica acta.

Dihydroxy-acid dehydratase, a [4Fe-4S] cluster-containing enzyme in Escherichia coli: effects of intracellular superoxide dismutase on its inactivation by oxidant stress.

O. Brown, J. Fee, B. Draczynska-Lusiak, 1995, Archives of biochemistry and biophysics.

An investigation of Chromatium vinosum high-potential iron-sulfur protein by EPR and Mossbauer spectroscopy; evidence for a freezing-induced dimerization in NaCl solutions.

C. Humblet, J. Dunbar, W. Hagen, 1991, Biochimica et biophysica acta.

High Resolution Structure of the ba3 Cytochrome c Oxidase from Thermus thermophilus in a Lipidic Environment

Wei Liu, V. Katritch, V. Cherezov, 2011, PloS one.

The circumsphere as a tool to assess distortion in [4Fe-4S] atom clusters

D. Case, R. A. Torres, C. Stout, 2003, JBIC Journal of Biological Inorganic Chemistry.

Characterization of 3-iron ferredoxins by means of the linear electric field effect in EPR.

H. Beinert, W. Orme-Johnson, N. Orme-Johnson, 1983, The Journal of biological chemistry.

THE ROLE OF SUPEROXIDE IN THE INDUCTION OF SUPEROXIDE DISMUTASE AND OXYGEN TOXICITY1

A. C. Lees, F. Neidhardt, P. Bloch, 1979 .

Characterization of phosphatidylinositol-specific phospholipase C defects associated with thrombin-induced mitogenesis.

S. Rhee, J. Fee, D. F. Silbert, 1990, The Journal of biological chemistry.

Linking Chemical Electron–Proton Transfer to Proton Pumping in Cytochrome c Oxidase: Broken-Symmetry DFT Exploration of Intermediates along the Catalytic Reaction Pathway of the Iron–Copper Dinuclear Complex

R. Walker, Louis Noodleman, J. Fee, 2014, Inorganic chemistry.

Toward a chemical mechanism of proton pumping by the B-type cytochrome c oxidases: application of density functional theory to cytochrome ba3 of Thermus thermophilus.

D. Case, Louis Noodleman, J. Fee, 2008, Journal of the American Chemical Society.

Accommodation of two diatomic molecules in cytochrome bo: insights into NO reductase activity in terminal oxidases.

R. Gennis, J. Fee, Myat T. Lin, 2009, Biochemistry.

Magnetization of manganese superoxide dismutase from Thermus thermophilus.

J. Fee, J. Peterson, E. Day, 1991, Biochimica et biophysica acta.

Structural changes that occur upon photolysis of the Fe(II)(a3)-CO complex in the cytochrome ba(3)-oxidase of Thermus thermophilus: a combined X-ray crystallographic and infrared spectral study demonstrates CO binding to Cu(B).

Bin Liu, C. Stout, S. M. Soltis, 2012, Biochimica et Biophysica Acta.

Rieske protein from Thermus thermophilus: 15N NMR titration study demonstrates the role of iron-ligated histidines in the pH dependence of the reduction potential.

W. M. Westler, J. Markley, Jikui Song, 2006, Journal of the American Chemical Society.

Exploring the proton pump and exit pathway for pumped protons in cytochrome ba3 from Thermus thermophilus

James Hemp, Robert B. Gennis, James A. Fee, 2012, Proceedings of the National Academy of Sciences.

Ligand access to the active site in Thermus thermophilus ba(3) and bovine heart aa(3) cytochrome oxidases.

C. Stout, J. Fee, I. Szundi, 2013, Biochemistry.

Mobility of Xe atoms within the oxygen diffusion channel of cytochrome ba(3) oxidase.

A. Deniz, C. Stout, J. Fee, 2012, Biochemistry.

Pulse Radiolysis Studies of Temperature Dependent Electron Transfers among Redox Centers in ba(3)-Cytochrome c Oxidase from Thermus thermophilus: Comparison of A- and B-Type Enzymes.

O. Farver, J. Fee, W. Antholine, 2010, Biochemistry.

Electron paramagnetic resonance studies of the soluble CuA protein from the cytochrome ba3 of Thermus thermophilus.

J. Fee, T. Vänngård, R. Aasa, 1996, Biophysical journal.

The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 Å resolution

H. Bellamy, D. McRee, E. Stura, 1999, Nature Structural Biology.

Multi-frequency EPR evidence for a binuclear CuA center in cytochrome c oxidase: studies with a 63Cu- and 65Cu-enriched, soluble domain of the cytochrome ba3 subunit II from Thermus thermophilus.

J. Fee, T. Vänngård, P. Doan, 1995, Biochemical and biophysical research communications.

Saturation behavior of superoxide dismutation catalyzed by the iron containing superoxide dismutase of E. coli B.

E. Fielden, P. O'Neill, J. Fee, 1981, Biochemical and biophysical research communications.

The two-state issue in the mixed-valence binuclear CuA center in cytochrome C oxidase and N2O reductase.

S. I. Gorelsky, E. Solomon, J. Fee, 2006, Journal of the American Chemical Society.

The Lost Horizon in Pleading under the Federal Rules of Civil Procedure

J. Fee, 1948 .

High-resolution structure of the soluble, respiratory-type Rieske protein from Thermus thermophilus: analysis and comparison.

A. Heine, D. McRee, C. Stout, 2003, Biochemistry.

Effect of redox state on the folding free energy of a thermostable electron-transfer metalloprotein: the CuA domain of cytochrome oxidase from Thermus thermophilus.

H. Gray, P. Wittung-Stafshede, J. Winkler, 1998, Biochemistry.

Some Spectroscopic Views of the CuA, Site in Cytochrome c Oxidase Preparations a

C. P. Barrett, G. George, A. Thomson, 1988, Annals of the New York Academy of Sciences.

Characterization of crystals of tetrameric manganese superoxide dismutase from Thermus thermophilus HB8.

T. B. Powers, W. Stallings, M. Ludwig, 1981, Journal of Biological Chemistry.

Purification and Characterization of the Rieske Iron-Sulfur Protein from Thermus thermophilus

Days, George, David, 2001 .

THE CUA DOMAIN OF CYTOCHROME BA3 FROM THERMUS THERMOPHILUS

H. Bellamy, D. McRee, E. Stura, 1999 .

Molecular Genetic and Protein Chemical Characterization of the Cytochrome ba3 from Thermus thermophilus HB8 (*)

M. Mather, A. Pastuszyn, J. Fee, 1995, The Journal of Biological Chemistry.

Fourier Transform Infrared And Resonance Raman Characterization Of Cytochrome Ba3 From Thermus Thermophilus

William H. Woodruff, Olof Einarsdottir, R. Brian Dyer, 1989, Photonics West - Lasers and Applications in Science and Engineering.

Respiratory proteins from the extremely thermophilic aerobic bacterium, Thermus thermophilus. Purification procedures for cytochromes c552, c555,549, and c1aa3 and chemical evidence for a single subunit cytochrome aa3.

R. Lorence, J. Fee, G. Tarr, 1984, The Journal of biological chemistry.

Conserved Glycine 232 in the Ligand Channel of ba3 Cytochrome Oxidase from Thermus thermophilus

C. Stout, J. Fee, I. Szundi, 2014, Biochemistry.

Cloning and Sequence Analysis of the Structural Gene for the bc1-Type Rieske Iron-Sulfur Protein from Thermus thermophilus HB8

S. Ackerman, D. Gatti, J. Fee, 1998, Journal of bioenergetics and biomembranes.

The rate-limiting step in O(2) reduction by cytochrome ba(3) from Thermus thermophilus.

D. Rousseau, T. Egawa, J. Fee, 2012, Biochimica et biophysica acta.