H. Beinert

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DNA Binding and Dimerization of the Fe−S-containing FNR Protein from Escherichia coli Are Regulated by Oxygen (*)

P. Kiley, B. Lazazzera, H. Beinert, 1996, The Journal of Biological Chemistry.

Crystal structures of aconitase with isocitrate and nitroisocitrate bound.

C. Stout, H. Beinert, M. Kennedy, 1993, Biochemistry.

Effect of ACTH on cholesterol side-chain cleavage in rat adrenal mitochondria.

G. S. Boyd, C. Jefcoate, E. Simpson, 1972, Biochemical and biophysical research communications.

On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. II. The electron-transferring flavoprotein.

F. L. Crane, H. Beinert, E. Steyn-Parvé, 1956, The Journal of biological chemistry.

On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase.

F. L. Crane, H. Beinert, D. E. Green, 1956, The Journal of biological chemistry.

Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins.

H. Beinert, 1983, Analytical biochemistry.

Electron carriers of cytochrome oxidase detectable by electron paramagnetic resonance and their relationship to those traditionally recognized in this enzyme.

H. Beinert, C. Hartzell, R. E. Hansen, 1973, Proceedings of the National Academy of Sciences of the United States of America.

Studies on the origin of the near-infrared (800-900 nm) absorption of cytochrome c oxidase.

H. Beinert, C. Hartzell, R. E. Hansen, 1980, Biochimica et biophysica acta.

Interaction of ubisemiquinone with a paramagnetic component in heart tissue.

H. Beinert, K. Schepler, R. Sands, 1975, Proceedings of the National Academy of Sciences of the United States of America.

Studies on succinic and DPNH dehydrogenase preparations by paramagnetic resonance (EPR) spectroscopy

H. Beinert, R. Sands, 1960 .

Evidence for a new type of iron containing electron carrier in mitochondria.

H. Beinert, W. Lee, W. Lee, 1961, Biochemical and biophysical research communications.

The number of iron atoms in the paramagnetic center (G =1.94) of reduced putidaredoxin, a nonheme iron protein.

H. Beinert, W. Orme-Johnson, I. C. Gunsalus, 1968, Proceedings of the National Academy of Sciences of the United States of America.

Copper A of cytochrome c oxidase, a novel, long-embattled, biological electron-transfer site.

H. Beinert, Helmut Beinert, 1997, European journal of biochemistry.

The soluble "high potential" type iron-sulfur protein from mitochondria is aconitase.

H. Beinert, F. Ruzicka, 1978, The Journal of biological chemistry.

Oxidation of reduced cytochrome c oxidase with 18O2. A search for mu-oxo-bridged metal species in the oxidized enzyme.

H. Beinert, M. O'Leary, R. Shaw, 1981, The Journal of biological chemistry.

Catalysis and Gene Regulation

H. Beinert, 2010 .

These are the Moments when we Live! From Thunberg Tubes and Manometry to Phone, Fax and Fedex

H. Beinert, 1995 .

Mode of substrate carboxyl binding to the [4Fe-4S]+ cluster of reduced aconitase as studied by 17O and 13C electron-nuclear double resonance spectroscopy.

B. Hoffman, H. Beinert, M. Kennedy, 1987, Proceedings of the National Academy of Sciences of the United States of America.

19th Sir Hans Krebs lecture. Engineering of protein bound iron-sulfur clusters. A tool for the study of protein and cluster chemistry and mechanism of iron-sulfur enzymes.

H. Beinert, M. Kennedy, 1989, European journal of biochemistry.

Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding.

R. Klausner, H. Beinert, M. Kennedy, 1992, Proceedings of the National Academy of Sciences of the United States of America.

The pattern of iron—sulfur centers in brown adipose tissue mitochondria: Preponderance of ETF dehydrogenase and invariance with the thermogenic state

T. Flatmark, H. Beinert, F. Ruzicka, 1976, FEBS Letters.

The extent of artificial redistribution of cytochrome c in rat liver homogenates.

H. Beinert, 1951, The Journal of biological chemistry.

Binding of cytosolic aconitase to the iron responsive element of porcine mitochondrial aconitase mRNA.

H. Zalkin, H. Beinert, M. Kennedy, 1992, Archives of biochemistry and biophysics.

New evidence for the occurrence of free radicals in flavoprotein catalysis.

H. Beinert, 1956, Biochimica et biophysica acta.

The state of cluster SH and S2- of aconitase during cluster interconversions and removal. A convenient preparation of apoenzyme.

H. Beinert, M. Kennedy, 1988, The Journal of biological chemistry.

Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding.

P. Kiley, H. Beinert, N. Khoroshilova, 1995, Proceedings of the National Academy of Sciences of the United States of America.

The active site sulfhydryl of aconitase is not required for catalytic activity.

G. Spoto, H. Beinert, M. Kennedy, 1988, The Journal of biological chemistry.

On the formation of the superoxide anion radical during the reaction of reduced iron-sulfur proteins with oxygen.

H. Beinert, W. Orme-Johnson, 1969, Biochemical and biophysical research communications.

Further Studies of an Intermediate in the Oxidation of Reduced Cytochrome c Oxidase by Oxygen

H. Beinert, R. Sands, R. Shaw, 1982 .

Resonance Raman spectroscopy of cytochrome c oxidase and electron transport particles with excitation near the Soret band.

D. Gill, H. Beinert, L. Rimai, 1973, Biochemical and biophysical research communications.

An EPR investigation of the products of the reaction of cytosolic and mitochondrial aconitases with nitric oxide.

H. Beinert, M. Kennedy, W. Antholine, 1997, The Journal of biological chemistry.

Studies on the cyclophorase system. XXV. Fatty acid oxidation in the rabbit liver system.

H. Beinert, V. Cheldelin, 1952, Biochimica et biophysica acta.

S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance.

G. H. Reed, P. Frey, H. Beinert, 1998, Biochemistry.

Evidence for the formation of a linear [3Fe-4S] cluster in partially unfolded aconitase.

H. Beinert, M. Kennedy, H. Merkle, 1984, The Journal of biological chemistry.

New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria.

H. Beinert, S. Albracht, Helmut Beinert, 1982, Biochimica et biophysica acta.

Iron-Sulfur Proteins Past Endeavors and Present Challenges

H. Beinert, 1982 .

EPR detectable electron acceptors in submitochondrial particles from beef heart with special reference to the iron-sulfur components of DPNH-ubiquinone reductase.

H. Beinert, W. Orme-Johnson, N. Orme-Johnson, 1971, Biochemical and Biophysical Research Communications - BBRC.

Non heme (iron-sulfur) proteins of Azotobacter vinelandii.

H. Beinert, D. Dervartanian, Y. Shethna, 1968, Biochemical and biophysical research communications.

CHAPTER 1 – Development of the Field and Nomenclature

H. Beinert, 1973 .

Components of cytochrome c oxidase detectable by EPR spectroscopy.

H. Beinert, C. Hartzell, Helmut Beinert, 1974, Biochimica et biophysica acta.

Mössbauer and EPR studies of activated aconitase: development of a localized valence state at a subsite of the [4Fe-4S] cluster on binding of citrate.

H. Beinert, M. Kennedy, E. Münck, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Micro methods for the quantitative determination of iron and copper in biological material.

H. Beinert, Mildred Van De Bogart, 1967, Methods in enzymology.

Spin-state changes in cytochrome P-450cam on binding of specific substrates.

H. Beinert, W. Orme-Johnson, J. Peisach, 1970, Proceedings of the National Academy of Sciences of the United States of America.

Anaerobic reductive titrations with solid diluted sodium dithionite in an apparatus suitable for EPR spectroscopy.

H. Beinert, W. Orme-Johnson, W. H. Orme-Johson, 1969, Analytical biochemistry.

14,15N, 13C, 57Fe, and 1,2H Q-band ENDOR study of Fe-S proteins with clusters that have endogenous sulfur ligands.

B. Oh, J. Markley, B. Hoffman, 1992, Biochemistry.

Trails of inquiry and thought leading toward today's bioenergetics.

H. Beinert, 1992, Biochimica et biophysica acta.

2H mims pulsed ENDOR of hydrogen bonds and exogenous ligands to the metal clusters of iron-sulfur proteins

B. Hoffman, H. Beinert, M. Kennedy, 1992 .

Mössbauer study of the inactive Fe3S4 and Fe3Se4 and the active Fe4Se4 forms of beef heart aconitase.

H. Beinert, M. Kennedy, E. Münck, 1989, Proceedings of the National Academy of Sciences of the United States of America.

17O electron nuclear double resonance characterization of substrate binding to the [4Fe-4S]1+ cluster of reduced active aconitase.

B. Hoffman, H. Beinert, M. Kennedy, 1986, The Journal of biological chemistry.

Properties of the copper associated with cytochrome oxidase as studied by paramagnetic resonance spectroscopy.

H. Beinert, D. E. Griffiths, R. Sands, 1962, The Journal of biological chemistry.

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.

The acetate activating enzyme system of heart muscle.

H. Beinert, D. E. Green, C. Ramakrishnan, 1953, The Journal of biological chemistry.

Iron–Sulfur Proteins

H. Beinert, 2004 .

Iron-sulfur proteins: ancient structures, still full of surprises

H. Beinert, 2000, JBIC Journal of Biological Inorganic Chemistry.

Identification of sulfur as component of the EPR signal at g = 1.94 by isotopic substitution

H. Beinert, W. Orme-Johnson, I. C. Gunsalus, 1967 .

Contributions of EPR spectroscopy to our knowledge of oxidative enzymes.

H. Beinert, G. Palmer, 1965, Advances in enzymology and related areas of molecular biology.

IDENTIFICATION BY ISOTOPIC SUBSTITUTION OF THE EPR SIGNAL AT G = 1.94 IN A NON-HEME IRON PROTEIN FROM AZOTOBACTER.

H. Beinert, P. W. Wilson, R. E. Hansen, 1964, Proceedings of the National Academy of Sciences of the United States of America.

OXIDATION-REDUCTION OF THE COPPER COMPONENT OF CYTOCHROME OXIDASE. KINETIC STUDIES WITH A RAPID FREEZING TECHNIQUE.

H. Beinert, G. Palmer, 1964, The Journal of biological chemistry.

Studies of the heme components of cytochrome c oxidase by EPR spectroscopy.

H. Beinert, B. V. van Gelder, B. F. Gelder, 1969, Biochimica et biophysica acta.

Purification and properties of two iron-sulfur proteins from Azotobacter vinelandii.

H. Beinert, D. Dervartanian, Y. Shethna, 1969, Biochimica et biophysica acta.

What Do We and What Don't We Know Today about Cytochrome c Oxidase?

H. Beinert, 1988, Annals of the New York Academy of Sciences.

Mitochondrial NADH dehydrogenase in iron‐deficient and iron‐repleted rat muscle: an EPR and work performance study

Y. Ohira, H. Beinert, L. Strause, 1982, British journal of haematology.

Micro methods for the quantitative determination of iron and copper in biological material.

H. Beinert, M. Van de Bogart, 1967, Analytical biochemistry.

Electron paramagnetic resonance-detectable electron acceptors in beef heart mitochondria. Reduced diphosphopyridine nucleotide ubiquinone reductase segment of the electron transfer system.

H. Beinert, N. Orme-Johnson, R. E. Hansen, 1974, The Journal of biological chemistry.

Special techniques for the preparation of samples for low-temperature EPR spectroscopy.

H. Beinert, W. Orme-Johnson, G. Palmer, 1978, Methods in enzymology.

Heterogeneity of paramagnetic species in two iron-sulfur proteins: Clostridium pasteurianum ferredoxin and milk xanthine oxidase.

H. Beinert, W. Orme-Johnson, 1969, Biochemical and biophysical research communications.

Overexpression of iron-responsive element-binding protein and its analytical characterization as the RNA-binding form, devoid of an iron-sulfur cluster.

R. Klausner, J. Basilion, H. Beinert, 1994, Archives of biochemistry and biophysics.

Characterization of the [4Fe-4S]+ cluster at the active site of aconitase by 57Fe, 33S, and 14N electron nuclear double resonance spectroscopy.

B. Hoffman, H. Beinert, M. Kennedy, 1990, Biochemistry.

17O, 1H, and 2H electron nuclear double resonance characterization of solvent, substrate, and inhibitor binding to the [4Fe-4S]+ cluster of aconitase.

B. Hoffman, H. Beinert, M. Kennedy, 1990, Biochemistry.

Incorporation of [35S]sulfide into the Fe-S cluster of aconitase.

H. Beinert, M. Kennedy, M. Emptage, 1984, The Journal of biological chemistry.

Reaction sites of rotenone, piericidin A, and amytal in relation to the nonheme iron components of NADH dehydrogenase.

J. Casida, H. Beinert, M. Gutman, 1970, Proceedings of the National Academy of Sciences of the United States of America.

Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase. XIV. Location of the sites of inhibition of rotenone, barbiturates, and piericidin by means of electron paramagnetic resonance spectroscopy.

H. Beinert, G. Palmer, D. J. Horgan, 1968, The Journal of biological chemistry.

Iron-sulfur components of succinate dehydrogenase: stoichiometry and kinetic behavior in activated preparations.

H. Beinert, B. Ackrell, T. Singer, 1975, European journal of biochemistry.

Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster.

P. Kiley, H. Beinert, 1998, FEMS microbiology reviews.

Studies on the cyclophorase system. XXI. Condensation reactions involving glycine.

H. Beinert, D. E. Green, N. Sarkar, 1952, Archives of biochemistry and biophysics.

Kinetic studies of succinate dehydrogenase by electron paramagnetic resonance spectroscopy.

H. Beinert, W. Orme-Johnson, C. Veeger, 1969, Biochimica et biophysica acta.

ELECTRON SPIN RELAXATION AS A PROBE FOR ACTIVE CENTERS OF PARAMAGNETIC ENZYME SPECIES

H. Beinert, W. Orme-Johnson, 1967 .

Spectroscopy of succinate dehydrogenases, a historical perspective.

H. Beinert, 2002, Biochimica et biophysica acta.

Bioinorganic Chemistry: A New Field or Discipline? Words, Meanings, and Reality

H. Beinert, 2002, The Journal of Biological Chemistry.

Preparation of cytochrome oxidase from beef heart.

H. Beinert, B. V. van Gelder, C. Hartzell, 1978, Methods in enzymology.

Structure and function of copper proteins : Report, on the fourth La Cura Conference held at Villa Giulia, Manziana, Rome, Italy, 4-8 September 1979

H. Beinert, 1980 .

Copper in biological systems. A report from the 6th Manziana Conference, September 23-27, 1990.

H. Beinert, Helmut Beinert, 1991, Journal of inorganic biochemistry.

The oxygen reactions of reduced cytochrome c oxidase. Position of a form with an unusual EPR signal in the sequence of early intermediates.

H. Beinert, R. E. Hansen, R. Shaw, 1979, Biochimica et biophysica acta.

A novel electron paramagnetic resonance signal of "oxygenated" cytochrome c oxidase.

H. Beinert, R. E. Hansen, R. Shaw, 1978, The Journal of biological chemistry.

STRUCTURE AND FUNCTION OF COPPER PROTEINS

H. Beinert, 1977 .

Copper in biological systems. A report from the 7th Manziana Conference, held at Santa Severa, September 11-15, 1995.

H. Beinert, 1996, Journal of inorganic biochemistry.

Studies of aldehyde oxidase by electron paramagnetic resonance spectroscopy. I. Spectra at equilibrium states.

K. Rajagopalan, H. Beinert, P. Handler, 1968, The Journal of biological chemistry.

DIRECT STUDIES ON THE ELECTRON TRANSFER SEQUENCE IN XANTHINE OXIDASE BY ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY. I. TECHNIQUES AND DESCRIPTION OF SPECTRA.

H. Beinert, R. Bray, G. Palmer, 1964, The Journal of biological chemistry.

DIRECT STUDIES ON THE ELECTRON TRANSFER SEQUENCE IN XANTHINE OXIDASE BY ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY. II. KINETIC STUDIES EMPLOYING RAPID FREEZING.

H. Beinert, R. Bray, G. Palmer, 1964, The Journal of biological chemistry.

Analysis of the electron paramagnetic resonance spectrum of the cobalamin intermediate in ribonucleotide reduction.

Raymond L. Blakley, H. Beinert, W. Orme-Johnson, 1976, Biochimica et biophysica acta.

Studies on the Metabolism of Administered Cytochrome C by the Aid of Iron-labeled Cytochrome.

H. Beinert, 1950, Science.

A gas-flow system for control of the temperature of an electron paramagnetic resonance sample at temperatures between 80 and 273 degrees Kelvin.

H. Beinert, R. E. Hansen, T. T. Kalal, 1967, Analytical biochemistry.

Multiple frequency EPR studies on three forms of oxidized cytochrome c oxidase.

H. Beinert, R. Sands, R. Shaw, 1983, Biochimica et biophysica acta.

Cytochrome c oxidase. Time dependence of optical and EPR spectral changes related to the 'oxygen-pulsed' form.

H. Beinert, R. Shaw, F. Armstrong, 1983, Biochimica et biophysica acta.

AN EXPERIMENTAL EVALUATION OF THE BRAY RAPID-FREEZING TECHNIQUE*

H. Beinert, G. Palmer, 1964 .

Dual-mode EPR spectrometry of O2-pulsed cytochrome c oxidase.

W. Hagen, H. Beinert, R. Sands, 1984, Biochimica et biophysica acta.

Insights Gained by EPR Spectroscopy into the Composition and Function of the Mitochondrial Respiratory Chain

H. Beinert, 1982 .

Non-heme components of electron transfer systems: interactions and conformational effects.

H. Beinert, 1982, Advances in experimental medicine and biology.

Diamine oxidase from pig kidney. Improved purification and properties.

A. Finazzi-Agro’, E. Chiancone, G. Rotilio, 1967, The Journal of biological chemistry.

ACONITASE AS IRON-SULFUR PROTEIN, ENZYME, AND IRON-REGULATORY PROTEIN

Helmut Beinert, C. Stout, H. Beinert, 1996 .

A spin-label study of the disposition of the Fe-S cluster with respect to the active center of aconitase.

K. Hideg, S. Eaton, G. Eaton, 1983, Biochimica et biophysica acta.

Iron-sulfur clusters: nature's modular, multipurpose structures.

H. Beinert, R. H. Holm, E Münck, 1997, Science.

An Eventful Life Around Flavins: Memoirs Dictated in the Last Weeks of his Life, August 1981

H. Beinert, P. Hemmerich, 1986 .

Kinetic studies on cytochrome c oxidase by combined epr and reflectance spectroscopy after rapid freezing.

H. Beinert, C. Hartzell, R. E. Hansen, 1976, Biochimica et biophysica acta.

Oxido-reductive titrations of cytochrome c oxidase followed by EPR spectroscopy.

H. Beinert, C. Hartzell, 1976, Biochimica et biophysica acta.

The magnetic susceptibility of cytochrome oxidase in the 4.2-1.5 K range.

H. Beinert, C. Hartzell, T. King, 1978, The Journal of biological chemistry.

Studies on the state of copper in native and modified human ceruloplasmin.

C. Kasper, H. Beinert, H. F. Deutsch, 1963, The Journal of biological chemistry.

Recent developments in the field of iron‐sulfur proteins

H. Beinert, 1990, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Engineering of protein bound iron‐sulfur clusters

H. Beinert, M. Kennedy, 1989 .

Iron-sulfur stoichiometry and structure of iron-sulfur clusters in three-iron proteins: evidence for [3Fe-4S] clusters.

H. Beinert, R. A. Scott, A. Thomson, 1983, Proceedings of the National Academy of Sciences of the United States of America.

IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins

P. Kiley, J. L. Giel, H. Beinert, 2001, Proceedings of the National Academy of Sciences of the United States of America.

A tribute to sulfur.

H. Beinert, 2000, European journal of biochemistry.

A mitochondrial iron protein with properties of a high-potential iron-sulfur protein.

H. Beinert, F. Ruzicka, 1974, Biochemical and biophysical research communications.

EPR studies of the cytochrome b-c 1 segment of the mitochondrial electron transfer system.

H. Beinert, N. Orme-Johnson, R. E. Hansen, 1971, Biochemical and biophysical research communications.

EVIDENCE FOR SEMIQUINONE-METAL INTERACTION IN METAL-FLAVOPROTEINS.

H. Beinert, P. Hemmerich, 1965, Biochemical and biophysical research communications.

CORRELATION OF ENZYMATIC ACTIVITY AND THE APPEARANCE OF THE EPR SIGNAL AT G = 1.94 IN NADH DEHYDROGENASE AND ITS THERMAL BREAKDOWN PRODUCTS.

H. Beinert, G. Palmer, T. Singer, 1963, Biochemical and biophysical research communications.

The role of Fe-S proteins in sensing and regulation in bacteria.

P. Kiley, H. Beinert, 2003, Current opinion in microbiology.

Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae.

E. Craig, H. Beinert, B. Schilke, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae.

E. Craig, H. Beinert, Y. C. Cheng, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster.

P. Kiley, H. Beinert, H Beinert, 1998, FEMS microbiology reviews.

Substitution of Leucine 28 with Histidine in theEscherichia coli Transcription Factor FNR Results in Increased Stability of the [4Fe-4S]2+ Cluster to Oxygen*

P. Kiley, H. Beinert, N. Khoroshilova, 2000, The Journal of Biological Chemistry.

Fe-S proteins in sensing and regulatory functions.

P. Kiley, H. Beinert, 1999, Current opinion in chemical biology.

Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity.

P. Kiley, H. Beinert, N. Khoroshilova, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Three-iron clusters in iron-sulfur proteins.

H. Beinert, A. Thomson, 1983, Archives of biochemistry and biophysics.

Mössbauer studies of beef heart aconitase: evidence for facile interconversions of iron-sulfur clusters.

H. Beinert, M. Kennedy, B. Huynh, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Investigations on microbial sulfur respiration. Isolation, purification, and characterization of cellular components from Spirillum 5175.

H. Beinert, M. Kennedy, P. Kroneck, 1991, European journal of biochemistry.

Purification of a non-heme iron protein and other electron transport components from Azotobacter extracts.

H. Beinert, P. W. Wilson, Y. Shethna, 1966, Biochimica et biophysica acta.

Spectral Characteristics of Flavins at the Semiquinoid Oxidation Level1

H. Beinert, 1956 .

Structural Characterization of 3Fe Clusters in Fe-S Proteins by EXAFS

K. Hodgson, C. Stout, H. Beinert, 1984 .

A new iron-sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway.

H. Beinert, F. Ruzicka, 1977, The Journal of biological chemistry.

Factors controlling the turnover number of succinate dehydrogenase: a new look at an old problem.

H. Beinert, G. A. White, A. Vinogradov, 1976, Advances in experimental medicine and biology.

Kinetics of the reoxidation of succinate dehydrogenase.

H. Beinert, K. Folkers, B. Ackrell, 1977, Archives of biochemistry and biophysics.

EFFECT OF ACTH ON ADRENAL MITOCHONDRIAL CYTOCHROME P‐450 IN THE RAT *

C. Jefcoate, E. Simpson, H. Beinert, 1973, Annals of the New York Academy of Sciences.

A New Look at the Electron-Transfer System of Heart Mitochondria

H. Beinert, N. Orme-Johnson, R. E. Hansen, 1973 .

Relationship of the oxidation state of the iron-sulfur cluster of aconitase to activity and substrate binding.

W. Cleland, H. Beinert, R. Ramsay, 1981, Biochemistry.

AN IRON-SULFUR CLUSTER OF THE HIPIP TYPE AS A COMPONENT OF ACONITASE. A NEW AREA OF INVOLVEMENT OF IRON-SULFUR PROTEINS?

H. Beinert, F. Ruzicka, 1978 .

EPR spectroscopy of components of the mitochondrial electron-transfer system.

H. Beinert, 1978, Methods in enzymology.

The reaction of fluorocitrate with aconitase and the crystal structure of the enzyme-inhibitor complex.

C. Stout, H. Beinert, M. Kennedy, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Localized Valence States in Iron-Sulfur Clusters and Their Possible Relationship to the Ability of Iron-Sulfur Clusters to Catalyze Reactions other than Electron Transfer

H. Beinert, 1987 .

The high potential iron-sulfur cluster of aconitase is a binuclear iron-sulfur cluster.

H. Beinert, F. Ruzicka, R. H. Holm, 1979, The Journal of biological chemistry.

[Nomenclature of enzymes in fatty acid metabolism].

S. Ochoa, O. Hoffmann-Ostenhof, H. Beinert, 1956, Biochemische Zeitschrift.

Aconitase, a two‐faced protein: enzyme and iron regulatory factor 1 2

H. Beinert, M. Kennedy, M C Kennedy, 1993, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Iron-sulfur proteins, the most numerous and most diversified components of the mitochondrial electron transfer system.

H. Beinert, 1976, Advances in experimental medicine and biology.

The acetoacetate activation and cleavage enzyme system.

H. Beinert, D. E. Green, D. Goldman, 1953, The Journal of biological chemistry.

A LINK BETWEEN FATTY ACYL CoA DEHYDROGENASE AND CYTOCHROME c: A NEW FLAVIN ENZYME1

F. L. Crane, H. Beinert, 1954 .

A METHOD FOR PURIFICATION OF COENZYME A

H. Beinert, D. E. Green, R. Handschumacher, 1952 .

A method for the purification of coenzyme A from yeast.

H. Beinert, D. E. Green, R. Handschumacher, 1953, The Journal of biological chemistry.

Further characterization of a photosystem-II particle isolated from spinach chloroplasts by triton treatment: the reaction-center components.

B. Kê, H. Beinert, S. Sahu, 1974, Biochimica et biophysica acta.

A new membrane iron-sulfur flavoprotein of the mitochondrial electron transfer system. The entrance point of the fatty acyl dehydrogenation pathway?

H. Beinert, F. Ruzicka, 1975, Biochemical and biophysical research communications.

Electron paramagnetic resonance-detectable electron acceptors in beef heart mitochondria. Ubihydroquinone-cytochrome c reductase segment of the electron transfer system and complex mitochondrial fragments.

H. Beinert, N. Orme-Johnson, R. E. Hansen, 1974, The Journal of biological chemistry.

The role of iron in the activation-inactivation of aconitase.

H. Beinert, M. Kennedy, J. Dreyer, 1983, The Journal of biological chemistry.

On the function of copper in cytochrome oxidase

H. Beinert, R. Sands, 1959 .

Role of the Mitochondrial Hsp70s, Ssc1 and Ssq1, in the Maturation of Yfh1

E. Craig, H. Beinert, Maikke B. Ohlson, 2000, Molecular and Cellular Biology.

The mechanism of action of ethanolamine ammonia-lyase, a B-12-dependent enzyme. The participation of paramagnetic species in the catalytic deamination of 2-aminopropanol.

H. Beinert, W. Orme-Johnson, B. Babior, 1974, The Journal of biological chemistry.

Cobamides and ribonucleotide reduction. XII. The electron paramagnetic resonance spectrum of "active coenzyme B12".

Raymond L. Blakley, H. Beinert, W. Orme-Johnson, 1974, The Journal of biological chemistry.

Redox control of gene expression involving iron‐sulfur proteins. Change of oxidation‐state or assembly/disassembly of Fe‐S clusters?

P. Kiley, H. Beinert, 1996, FEBS letters.

Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein

H. Beinert, M. Kennedy, G A Blondin, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Comments on "the interpretation of the EPR and Mössbauer spectra of two-iron, one-electron iron-sulfur proteins".

A. Bearden, H. Beinert, W. Orme-Johnson, 1971, Biochemical and biophysical research communications.

The two-iron ferredoxins in spinach, parsley, pig adrenal cortex, Azotobacter vinelandii, and Clostridium pasteurianum: studies by magnetic field Mössbauer spectroscopy.

A. Bearden, H. Beinert, W. Orme-Johnson, 1971, Biochimica et biophysica acta.

On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. VI. Isolation and properties of stable enzyme-substrate complexes.

H. Beinert, E. Steyn-Parvé, 1958, The Journal of biological chemistry.

On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl coA dehydrogenase.

F. L. Crane, H. Beinert, J. G. Hauge, 1956, The Journal of biological chemistry.

Some properties of an apoceruloplasmin-like protein in human serum.

H. Beinert, W. Orme-Johnson, R. Carrico, 1969, The Journal of biological chemistry.

A reappraisal of copper depletion from cytochrome c oxidase.

K. Ganapathy, H. S. Mason, H. Beinert, 1970, The Journal of biological chemistry.

APPEARANCE OF SULFHYDRYL GROUPS DURING GROWTH OF BACILLUS GLOBIGII

H. Beinert, L. Mortenson, 1953, Journal of bacteriology.

Optical and EPR characterization of different species of active and inactive aconitase.

H. Beinert, M. Kennedy, M. Emptage, 1983, The Journal of biological chemistry.

Synthesis of butyryl-coenzyme A by reversal of the oxidative pathway.

H. Beinert, P. Stansly, 1953, Biochimica et Biophysica Acta.

Evidence for an intermediate in the oxidation-reduction of flavoproteins.

H. Beinert, 1957, The Journal of biological chemistry.

Electron paramagnetic resonance studies of iron reduction and semiquinone formation in metalloflavoproteins.

K. Rajagopalan, H. Beinert, P. Handler, 1962, Biochemical and Biophysical Research Communications - BBRC.

CHAPTER 3 – Iron–Sulfur Centers of the Mitochondrial Electron Transfer System—Recent Developments

H. Beinert, 1977 .

An EPR Investigation of the Products of the Reaction of Cytosolic and Mitochondrial Aconitases with Nitric Oxide*

H. Beinert, M. Kennedy, W. Antholine, 1997, The Journal of Biological Chemistry.

Superoxide destroys the [2Fe-2S]2+ cluster of FNR from Escherichia coli.

Victoria R. Sutton, P. Kiley, H. Beinert, 2004, Biochemistry.

Studies on the spin-spin interaction between flavin and iron-sulfur cluster in an iron-sulfur flavoprotein.

H. Beinert, R. Sands, W. Dunham, 1986, Biochimica et biophysica acta.

Mechanistic studies on the dehydrogenases of methylotrophic bacteria. 2. Kinetic studies on the intramolecular electron transfer in trimethylamine and dimethylamine dehydrogenase.

D. J. Steenkamp, H. Beinert, 1982, The Biochemical journal.

Mechanistic studies on the dehydrogenases of methylotrophic bacteria. 1. The influence of substrate binding to reduced trimethylamine dehydrogenase on the intramolecular electron transfer between its prosthetic groups.

D. J. Steenkamp, H. Beinert, 1982, The Biochemical journal.

Studies on the cyclophorase system: XXVII. Cyclophorase activity in a non-mitochondrial system of pig heart muscle☆☆☆

H. Beinert, D. E. Green, D. Goldman, 1953 .

On the function of iron in DPNH cytochrome c reductase

H. Beinert, R. Sands, 1959 .

Use of Electron Paramagnetic Resonance Spectroscopy in Investigations of Functional Metal Components in Micro-Organisms

D. Nicholas, H. Beinert, P. W. Wilson, 1962, Nature.

DIFFUSE REFLECTANCE SPECTROSCOPY OF FROZEN SAMPLES AS AN ADJUNCT TO LOW-TEMPERATURE ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY.

H. Beinert, G. Palmer, 1964, Analytical biochemistry.

Studies on mitochondria and submitochondrial particles by paramagnetic resonance (EPR) spectroscopy

H. Beinert, R. Sands, 1960 .

Kinetic Studies on Reduced Diphosphopyridine Nucleotide Dehydrogenase by Electron Paramagnetic Resonance Spectroscopy

H. Beinert, G. Palmer, T. Singer, 1965 .

Reductive titrations of iron-sulfur proteins containing two to four iron atoms.

H. Beinert, W. Orme-Johnson, 1969, The Journal of biological chemistry.

Looking at enzymes in action in the 1950s

H. Beinert, 1994, Protein science : a publication of the Protein Society.

[59] Electron-transferring flavoproteins from pig liver and beef heart

H. Beinert, William H. Lee, 1963 .

ON THE LIGAND FIELD OF REDOX ACTIVE NON-HEME IRON IN PROTEINS.

H. Beinert, P. Hemmerich, C. Veeger, 1965, Biochimica et biophysica acta.

Piericiden A sensitivity, site 1 phosphorylation, and reduced nicotinamide adenine dinucleotide dehydrogenase during iron-limited growth of Candida utilis.

H. Beinert, S. Grossman, T. Singer, 1975, The Journal of biological chemistry.

Heterogeneity in an isolated membrane protein Has the ‘authentic cytochrome oxidase’ been identified?

H. Beinert, R. A. Scott, G. Babcock, 1988, FEBS letters.

The Iron Responsive Element (IRE), the Iron Regulatory Protein (IRP), and Cytosolic Aconitase

H. Beinert, M. Kennedy, R. Eisenstein, 1998 .

The functional identity of the electron-transferring flavoproteins of the fatty acyl coenzyme A and sarcosine dehydrogenase systems.

H. Beinert, W. R. Frisell, 1962, The Journal of biological chemistry.

Mössbauer studies of aconitase. Substrate and inhibitor binding, reaction intermediates, and hyperfine interactions of reduced 3Fe and 4Fe clusters.

H. Beinert, M. Kennedy, H. Merkle, 1985, The Journal of biological chemistry.

The Metabolic Lesion in Iron Deficient Muscle

Y. Ohira, H. Beinert, L. Strause, 1981 .

Interrelations of reconstitution activity, reactions with electron acceptors, and iron-sulfur centers in succinate dehydrogenase.

H. Beinert, A. Vinogradov, B. Ackrell, 1977, Archives of biochemistry and biophysics.

EPR studies on the mechanism of action of succinate dehydrogenase in activated preparations.

H. Beinert, 1974, Biochemical and biophysical research communications.

Catalytic activity and EPR signals of DPNH dehydrogenase in relation to the acquisition and loss of piericidin sensitivity and of coupling site 1.

H. Beinert, S. Grossman, T. Singer, 1973, Biochemical and biophysical research communications.

Relation of the respiratory chain-linked reduced nicotinamide--adenine dinucleotide dehydrogenase to energy-coupling site 1.

H. Beinert, M. Gutman, T. Singer, 1972, Biochemistry.

AN ATTEMPT AT QUANTITATION OF THE SHARP LIGHT-INDUCED ELECTRON PARAMAGNETIC RESONANCE SIGNAL IN PHOTOSYNTHETIC MATERIALS.

H. Beinert, B. Kok, 1964, Biochimica et biophysica acta.

Oxidation-reduction potentials of bound iron-sulfur proteins of photosystem I.

B. Kê, H. Beinert, R. E. Hansen, 1973, Proceedings of the National Academy of Sciences of the United States of America.

Kinetics of appearance and disappearance of light-induced EPR signals of P700+ and iron-sulfur proteins(s) at low temperature.

H. Beinert, R. E. Hansen, W. D. Hamilton, 1974, Biochimica et biophysica acta.

Investigations on microbial sulfur respiration

H. Beinert, M. Kennedy, P. Kroneck, 1988, Archives of Microbiology.

The light induced electron paramagnetic resonance signal of photocatalyst P700.

H. Beinert, G. Hoch, B. Kok, 1962, Biochemical and biophysical research communications.

1. Activation and reduction of elemental sulfur in several strains of eubacteria

H. Beinert, M. Kennedy, P. Kroneck, 1988 .

Cluster Structure and H-Bonding in Native, Substrate-Bound, and 3Fe Forms of Aconitase as Determined by Resonance Raman Spectroscopy

H. Beinert, M. Kennedy, R. Czernuszewicz, 1994 .

Crystal structures of aconitase with trans-aconitate and nitrocitrate bound.

C. Stout, H. Beinert, M. Kennedy, 1993, Journal of molecular biology.

The Role of S‐Adenosylmethionine as a Poor Man's Adenosylcobalamin in the Reaction of Lysine 2,3‐Aminomutase

G. H. Reed, Christopher H. Chang, P. Frey, 2007 .

On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. V. Oxidation-reductions of the flavoproteins.

H. Beinert, E. Pagé, Helmut Beinert, 1957, The Journal of biological chemistry.

Fatty acid oxidation in soluble systems of mammalian origin: the beginnings.

H. Beinert, 1990, Progress in clinical and biological research.

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.

Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli.

P. Kiley, H. Beinert, E. Münck, 1998, Proceedings of the National Academy of Sciences of the United States of America.

On the identity of the high spin heme components of cytochrome c oxidase.

H. Beinert, R. Shaw, 1977, Biochimica et biophysica acta.

Attachment to split-beam spectrophotometer for absorbance recording in round tubes of small diameter.

H. Beinert, B. V. van Gelder, R. E. Hansen, 1970, Analytical biochemistry.

Responses of the a3 component of cytochrome c oxidase to substrate and ligand addition.

H. Beinert, R. E. Hansen, R. Shaw, 1978, Biochimica et biophysica acta.

ELECTRON‐NUCLEAR AND ELECTRON‐ELECTRON SPIN INTERACTIONS IN THE STUDY OF ENZYME STRUCTURE AND FUNCTION*

H. Beinert, W. Orme-Johnson, 1969, Annals of the New York Academy of Sciences.

The reconstruction of the fatty acid oxidizing system of animal tissues.

S. Wakil, H. Beinert, D. E. Green, 1953 .

Extended x-ray absorption fine structure of copper in cytochrome c oxidase: Direct evidence for copper-sulfur ligation.

H. Gray, H. Beinert, R. A. Scott, 1981, Proceedings of the National Academy of Sciences of the United States of America.

Studies on the fatty acid oxidizing system of animal tissues. II. beta-Ketoacyl derivatives of coenzyme A.

H. Beinert, 1953, Journal of Biological Chemistry.

The light induced EPR signal of photocatalyst P700. II. Two light effects.

H. Beinert, B. Kok, 1962, Biochemical and biophysical research communications.

A survey of EPR-detectable components in sulfur-reducing bacteria

H. Beinert, H. Merkle, R. Bache, 1983 .

Molecular weight of beef heart aconitase and stoichiometry of the components of its iron-sulfur cluster.

H. Beinert, M. Kennedy, L. Rydén, 1984, The Journal of biological chemistry.

Evidence for the identity of P430 of Photosystem I and chloroplast-bound iron-sulfur protein.

B. Kê, H. Beinert, 1973, Biochimica et biophysica acta.

Kinetic Analysis of the Oxidative Conversion of the [4Fe-4S]2+ Cluster of FNR to a [2Fe-2S]2+ Cluster

Victoria R. Sutton, P. Kiley, H. Beinert, 2004, Journal of bacteriology.

Crystals and structures of cytochrome c oxidases--the end of an arduous road.

H. Beinert, 1995, Chemistry & biology.

Cytochrome C Labeled With Radioactive Iron.

H. Beinert, H. Maier-Leibnitz, 1948, Science.

On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. VII. The nature of the green color of butyryl dehydrogenase.

H. Beinert, E. Steyn-Parvé, 1958, The Journal of biological chemistry.

Asymmetric labeling of acetoacetate by enzymatic acetyl exchange with acetyl coenzyme A.

H. Beinert, P. Stansly, 1953, The Journal of biological chemistry.

Evidence for a Novel Three-Iron Center in Two Ferredoxins and Aconitase

H. Beinert, W. Orme-Johnson, J. Moura, 1982 .

Electron spin echo studies of cytochrome c oxidase.

H. Beinert, W. Mims, J. Peisach, 1980, The Journal of biological chemistry.

Electron paramagnetic resonance of heme at intermediate oxidation states of cytochrome c oxidase.

H. Beinert, W. Orme-Johnson, B. V. van Gelder, 1967, Proceedings of the National Academy of Sciences of the United States of America.

Xanthine oxidase, a molybdo-flavoprotein.

H. Beinert, D. E. Green, 1953, Biochimica et Biophysica Acta.

Electron Paramagnetic Resonance-detectable Electron Acceptors in Beef Heart Mitochondria UBIHYDROQUINONE-CYTOCHROME c REDUCTASE SEGMENT OF THE ELECTRON TRANSFER SYS- TEM AND COMPLEX MITOCHONDRIAL FRAGMENTS*

H. Beinert, N. Orme-Johnson, R. E. Hansen, 2002 .

[73] Acyl dehydrogenases from pig and beef liver and beef heart: RCH2CH2COSCoA − 2H+ − 2e- ⇆ RCHCHCOSCoA

H. Beinert, 1962 .

Magnetic circular dichroism study of the selenium-substituted form (Fe3Se4) of bovine heart aconitase.

H. Beinert, M. Kennedy, A. Thomson, 1995, The Biochemical journal.

Mutational analysis of active site residues in pig heart aconitase.

H. Zalkin, H. Beinert, M. Kennedy, 1992, The Journal of biological chemistry.

Iron-sulfur cluster 3 of beef heart succinate-ubiquinone oxidoreductase is a 3-iron cluster.

H. Beinert, W. Mims, J. Peisach, 1984, The Journal of biological chemistry.

Aconitase as Ironminus signSulfur Protein, Enzyme, and Iron-Regulatory Protein.

C. Stout, H. Beinert, M. Kennedy, 1996, Chemical reviews.

Studies of aldehyde oxidase by electron paramagnetic resonance spectroscopy. II. Kinetic studies by rapid freezing.

K. Rajagopalan, H. Beinert, P. Handler, 1968, Journal of Biological Chemistry.

On the sulfur components of iron-sulfur proteins. I. The number of acid-labile sulfur groups sharing an unpaired electron with iron.

H. Beinert, W. Orme-Johnson, I. C. Gunsalus, 1968, Proceedings of the National Academy of Sciences of the United States of America.

Studies on dihydroorotate dehydrogenase by electron paramagnetic resonance spectroscopy. 3. Kinetic studies by rapid freezing.

H. Beinert, P. Handler, G. Palmer, 1968, The Journal of biological chemistry.

EPR on the P450(cam) system in the late 1960s with Gunny and his gang: insights concerning the structure of Fe-S proteins and the spin states of P450.

H. Beinert, 2003, Biochemical and biophysical research communications.

Metal site of nonheme (iron-sulfur) proteins.

H. Beinert, W. Orme-Johnson, I. C. Gunsalus, 1968, Science.

Syringe Ram for a Rapid-Freeze Sampling Instrument.

H. Beinert, R. E. Hansen, 1966 .

A quarter-century Biochemistry of copper with Bill Blumberg

H. Beinert, 2005, Biology of Metals.

Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein

H. Beinert, M. Kennedy, George A. BLONDINt, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Iron-sulphur clusters: agents of electron transfer and storage, and direct participants in enzymic reactions. Tenth Keilin memorial lecture.

H. Beinert, 1986, Biochemical Society transactions.