P. Boyer

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The ATP synthase--a splendid molecular machine.

P. Boyer, 1997, Annual review of biochemistry.

The role of sulfhydryl groups in the activity of D-glyceraldehyde 3-phosphate dehydrogenase.

P. Boyer, H. Segal, 1953, The Journal of biological chemistry.

Equilibrium Reaction Rates and Enzyme Mechanisms.

P. Boyer, E. Silverstein, H. Taniuchi, 1963 .

The control of pyruvate oxidation in a cell-free rat heart preparation by phosphate acceptors.

P. Boyer, M. Rabinovitz, M. Stulberg, 1951, Science.

The binding change mechanism for ATP synthase--some probabilities and possibilities.

P. Boyer, P D Boyer, 1993, Biochimica et biophysica acta.

Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase.

P. Boyer, Y. Milgrom, M. Murataliev, 1998, The Biochemical journal.

Catalytic site forms and controls in ATP synthase catalysis.

P. Boyer, P D Boyer, 2000, Biochimica et biophysica acta.

The unusual enzymology of ATP synthase.

P. Boyer, P D Boyer, 1987, Biochemistry.

2,4-Dinitrophenol causes a marked increase in the apparent Km of Pi and of ADP for oxidative phosphorylation.

P. Boyer, J. Rosing, C. Kayalar, 1976, Biochemical and biophysical research communications.

Reversal and Mechanism of Oxidative Phosphorylation

P. Boyer, A. Falcone, W. Harrison, 1954, Nature.

Oxygen transfer to AMP in the enzymic synthesis of the hydroxamate of tryptophan.

M. Hoagland, P. Zamecnik, P. Boyer, 1957, Biochimica et biophysica acta.

Subunits, composition, and related properties of succinyl coenzyme A synthetase.

P. Boyer, C. Leitzmann, J. Wu, 1970, Biochemistry.

The reaction mechanism of soy bean lipoxidase.

P. Boyer, A. Tappel, W. O. Lundberg, 1952, Journal of Biological Chemistry.

The catalytic activity of carboxypeptidase-degraded aldolase.

P. Boyer, A. Kowalsky, E. Drechsler, 1959, The Journal of biological chemistry.

A carboxypeptidase-O18-labeled water procedure for determination of CO OH-terminal residues and its application to aldolase.

P. Boyer, A. Kowalsky, 1960, Journal of Biological Chemistry.

EQUILIBRIUM REACTION RATES AND THE MECHANISMS OF BOVINE HEART AND RABBIT MUSCLE LACTATE DEHYDROGENASES.

P. Boyer, E. Silverstein, 1964, The Journal of biological chemistry.

Incorporation of water oxygens into intracellular nucleotides and RNA. I. Predominantly non-hydrolytic RNA turnover in Bacillus subtilis.

P. Boyer, S. Chaney, J. Duffy, 1972, Journal of molecular biology.

Exchange and localization of 3H and 180 from water and substrates by mitochondria.

P. Boyer, A. Kaplan, 1969, The Journal of biological chemistry.

Oxygen exchange in the gamma-phosphoryl group of protein-bound ATP during Mg2+-dependent adenosine triphosphatase activity of myosin.

Clive R. Bagshaw, P. Boyer, D. Trentham, 1975, Proceedings of the National Academy of Sciences of the United States of America.

New insights into one of nature's remarkable catalysts, the ATP synthase.

P. Boyer, 2001, Molecular cell.

Energy, Life, and ATP

P. Boyer, 1998, Bioscience reports.

Active/inactive state transitions of the chloroplast F1 ATPase are induced by a slow binding and release of Mg2+. Relationship to catalysis and control of F1 ATPases.

P. Boyer, Z. Xue, K. Guerrero, 1990, Journal of Biological Chemistry.

Control of ATP hydrolysis by ADP bound at the catalytic site of chloroplast ATP synthase as related to protonmotive force and magnesium

P. Boyer, Z. Du, 1989 .

Properties of chloroplast F1-ATPase partially modified by 2-azido adenine nucleotides, including demonstration of three catalytic pathways.

P. Boyer, Z. Xue, T. Mélèse, 1988, The Journal of biological chemistry.

Tightly bound 2-azido-adenine nucleotides at catalytic and noncatalytic sites of the rat liver F1 ATPase label adjacent tryptic peptides of the beta subunit.

P. Boyer, K. Guerrero, 1988, Biochemical and biophysical research communications.

Relationship of tightly bound ADP and ATP to control and catalysis by chloroplast ATP synthase.

P. Boyer, Z. Xue, T. Mélèse, 1988, Biochemistry.

Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase Photoaffinity labeling and peptide sequencing

P. Boyer, Z. Xue, C. G. Miller, 1987, FEBS letters.

Catalytic and regulatory effects of light intensity on chloroplast ATP synthase.

P. Boyer, S. Stroop, 1987, Biochemistry.

Bound adenosine 5'-triphosphate formation, bound adenosine 5'-diphosphate and inorganic phosphate retention, and inorganic phosphate oxygen exchange by chloroplast adenosinetriphosphatase in the presence of Ca2+ or Mg2+.

P. Boyer, D. Wu, 1986, Biochemistry.

Oxygen and deuterium exchanges show reversal of catalytic steps of citrate synthase: catalytic cooperativity is not observed

P. Boyer, J. A. Myers, 1984 .

Probes of catalytic site cooperativity during catalysis by the chloroplast adenosine triphosphate and the adenosine triphosphate synthase.

P. Boyer, W. Kohlbrenner, 1983, The Journal of biological chemistry.

Properties of ATP tightly bound to catalytic sites of chloroplast ATP synthase.

P. Boyer, L. T. Smith, G. Rosen, 1983, The Journal of biological chemistry.

Subunit interaction during catalysis. ATP modulation of catalytic steps in the succinyl-CoA synthetase reaction.

P. Boyer, C. Janson, G. Bild, 1980, The Journal of biological chemistry.

Oxygen-18 probes of enzymic reactions of phosphate compounds.

P. Boyer, D. Hackney, K. Stempel, 1980, Methods in enzymology.

Demonstration and quantitation of catalytic and noncatalytic bound ATP in submitochondrial particles during oxidative phosphorylation.

P. Boyer, M. Gresser, G. Rosen, 1979, The Journal of biological chemistry.

Assessment of total catalytic sites and the nature of bound nucleotide participation in photophosphorylation.

P. Boyer, M. Gresser, G. Rosen, 1979, The Journal of biological chemistry.

The formation of enzyme-bound and medium pyrophosphate and the molecular basis of the oxygen exchange reaction of yeast inorganic pyrophosphatase.

P. Boyer, C. Janson, C. Degani, 1979, The Journal of biological chemistry.

Occurrence and significance of oxygen exchange reactions catalyzed by mitochondrial adenosine triphosphatase preparations.

P. Boyer, R. Hutton, G. Choate, 1979, The Journal of biological chemistry.

Effect of actin concentration on the intermediate oxygen exchange of myosin; relation to the refractory state and the mechanism of exchange.

P. Boyer, J. Sleep, 1978, Biochemistry.

Characterization of phosphate oxygen exchange reactions catalyzed by myosin through measurement of the distribution of 18-O-labeled species.

P. Boyer, D. Hackney, J. Sleep, 1978, The Journal of biological chemistry.

Subunit interaction during catalysis. Implications of concentration dependency of oxygen exchanges accompanying oxidative phosphorylation for alternating site cooperativity.

P. Boyer, D. Hackney, 1978, The Journal of biological chemistry.

Dynamic reversal of enzyme carboxyl group phosphorylation as the basis of the oxygen exchange catalyzed by sarcoplasmic reticulum adenosine triphosphatase.

P. Boyer, D. Hackney, L. de Meis, 1977, Biochemistry.

Probes of initial phosphorylation events in ATP synthesis by chloroplasts.

P. Boyer, D. J. Smith, B. O. Stokes, 1976, The Journal of biological chemistry.

A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport

P. Boyer, 1975, FEBS letters.

Energy transduction and proton translocation by adenosine triphosphatases

P. Boyer, 1975, FEBS letters.

Isotopic probes of catalytic steps of myosin adenosine triphosphatase.

P. Boyer, R. G. Wolcott, 1975, Journal of supramolecular structure.

Refinements in oxygen-18 methodology for the study of phosphorylation mechanisms.

P. Boyer, K. Stempel, 1986, Methods in enzymology.

Conformational coupling in oxidative phosphorylation and photophosphorylation

P. Boyer, 1977 .

The rapid labeling of adenosine triphosphate by 32P-labeled inorganic phosphate and the exchange of phosphate oxygens as related to conformational coupling in oxidative phosphorylation.

P. Boyer, R. L. Cross, 1975, Biochemistry.

Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic Mercurials

P. Boyer, 1954 .

Mechanism of the enzyme-catalyzed bioluminescent oxidation of coelenterate-type luciferin.

M. J. Cormier, P. Boyer, R. Hart, 1978, Biochemical and biophysical research communications.

Isotope exchange probes and enzyme mechanisms

P. Boyer, 1978 .

Mechanisms of enzyme control as probed by equilibrium exchange rates: patterns of modifier effects with a two substrate, two product system.

P. Boyer, F. Wedler, 1973, Journal of theoretical biology.

Occurrence and characteristics of 18 O exchange reactions catalyzed by sodium- and potassium-dependent adenosine triphosphatases.

P. Boyer, A. Dahms, 1973, The Journal of biological chemistry.

Cystein oxygenase. II. Studies on the mechanism of the reaction with 18oxygen.

P. Boyer, J. Lombardini, T. Singer, 1969, The Journal of biological chemistry.

The effect of 6-deoxy-6-fluoro-d-glucose on yeast fermentation and on hexokinase.

P. Boyer, E. Blakley, 1955, Biochimica et biophysica acta.

Inorganic orthophosphate activation and adenosine diphosphate as the primary phosphoryl acceptor in oxidative phosphorylation.

P. Boyer, R. D. Hill, 1967, The Journal of biological chemistry.

A borohydride reduction method for characterization of the acyl phosphate linkage in proteins and its application to sarcoplasmic reticulum adenosine triphosphatase.

P. Boyer, C. Degani, Chemda Degani, 1973, The Journal of biological chemistry.

THE ELECTROPHORETIC MOBILITY OF HUMAN SERUM ALBUMIN AS AFFECTED BY LOWER FATTY ACID SALTS

P. Boyer, J. M. Luck, G. A. Ballou, 1945 .

THE HEAT COAGULATION OF HUMAN SERUM ALBUMIN

P. Boyer, J. M. Luck, G. A. Ballou, 1944 .

PROBES OF ENERGY INPUT IN ATP FORMATION BY OXIDATIVE PHOSPHORYLATION

P. Boyer, J. Rosing, C. Kayalar, 1976 .

The preparation and characterization of 1-phosphohistidine and 3-phosphohistidine.

P. Boyer, R. W. Moyer, D. Hultquist, 1966, Biochemistry.

The apparent independence of the phosphorylation and water formation reactions from the oxidation reactions of oxidative phosphorylation.

P. Boyer, R. Mitchell, L. Bieber, 1966, Journal of Biological Chemistry.

RELATIONSHIPS OF CA++ TO "PROTEIN-BOUND" PHOSPHATE FRACTIONS OF MITOCHONDRIA.

P. Boyer, A. Norman, L. Bieber, 1965, The Journal of biological chemistry.

Uses and limitations of measurements of rates of isotopic exchange and incorporation in catalyzed reactions.

P. Boyer, P D BOYER, 1959, Archives of biochemistry and biophysics.

P. Boyer, 1967 .

Substrate interchanges and oxygen transfers catalyzed by glutamine synthetase at equilibrium.

P. Boyer, D. Graves, 1962, Biochemistry.

Hypotheses for and some kinetic studies with glutamine synthetase and acetate thiokinase.

R. C. Mills, H. Fromm, P. Boyer, 1959, Archives of biochemistry and biophysics.

Mechanism of the enzyme--catalyzed oxidation of Cypridina and firefly luciferins studied by means of 17O2 and H218O1.

P. Boyer, M. Deluca, F. I. Tsuji, 1977, Biochemical and biophysical research communications.

INSTABILITY OF PYRUVATE-C-14 IN AQUEOUS SOLUTION AS DETECTED BY ENZYMIC ASSAY.

P. Boyer, E. Silverstein, 1964, Analytical biochemistry.

Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase.

P. Boyer, J. Kachmar, 1953, The Journal of biological chemistry.

Properties of a polar 32P-phospholipid isolated from a particulate mitochondrial ATPase.

P. Boyer, A. Tzagoloff, K. H. Byington, 1968, Archives of biochemistry and biophysics.

Sulfhydryl Groups in Relation to Aldolase Structure and Catalytic Activity1

P. Boyer, A. Swenson, 1957 .

The enzymes. Vol. VII. Elimination and addition, aldol cleavage and condensation, other C-C cleavage, phosphorolysis, hydrolysis (fats, glycosides).

P. Boyer, 1972 .

Interconversion of α-tocopherol and its oxidation products

P. Boyer, J. Gander, W. Harrison, 1956 .

Detection of bound phosphohistidine in E. coli succinate thiokinase.

P. Boyer, G. Kreil, 1964, Biochemical and biophysical research communications.

Detection of a Possible Intermediate in Oxidative Phosphorylation

P. Boyer, M. Deluca, C. Suelter, 1961, Nature.

Simple procedure for conversion of oxygen of orthophosphate or water to carbon dioxide for oxygen-18 determination

P. Boyer, D. Graves, M. Dempsey, 1961 .

The inhibition of pyruvate kinase by ATP: a Mg++ buffer system for use in enzyme studies.

P. Boyer, 1969, Biochemical and biophysical research communications.

The magnesium activation of pyrophosphatase.

P. Boyer, M. Stulberg, E. A. Robbins, 1955, Archives of biochemistry and biophysics.

The Change in Reduced Diphosphopyridine Nucleotide (DPNH) Fluorescence upon Combination with Liver Alcohol Dehydrogenase (ADH).

P. Boyer, B. Thorell, H. Theorell, 1956 .

The preparation, properties, and reactions of succinyl coenzyme A synthetase and its phosphorylated form.

P. Boyer, W. A. Bridger, R. Ramaley, 1967, The Journal of biological chemistry.

On the mechanism of the enzymatic synthesis of lactose.

P. Boyer, J. Gander, W. Petersen, 1956, Archives of biochemistry and biophysics.

Mechanism of the propionyl carboxylase reaction. II. Isotopic exchange and tracer experiments.

L. F. Hass, S. Ochoa, P. Boyer, 1962, The Journal of biological chemistry.

EQUILIBRIUM REACTION RATES AND THE MECHANISMS OF LIVER AND YEAST ALCOHOL DEHYDROGENASE.

P. Boyer, E. Silverstein, 1964, The Journal of biological chemistry.

Products of the lipoxidase-catalyzed oxidation of sodium linoleate

P. Boyer, W. O. Lundberg, O. S. Privett, 1955 .

Incorporation of water oxygens into intracellular nucleotides and RNA. II. Predominantly hydrolytic RNA turnover in Escherichia coli.

P. Boyer, S. Chaney, 1972, Journal of molecular biology.

Energization of active transport by Escherichia coli.

P. Boyer, W. Klein, 1972, The Journal of biological chemistry.

CHARACTERISTICS OF BOUND PHOSPHOHISTIDINE LABELING IN MITOCHONDRIA.

P. Boyer, A. Norman, J. Duffy, 1965, The Journal of biological chemistry.

Quantitative appraisals of possible catalytic intermediates in the succinyl coenzyme A synthetase reaction.

P. Boyer, J. Robinson, R. W. Benson, 1969, Biochemistry.

Bioenergetic coupling to protonmotive force: should we be considering hydronium ion coordination and not group protonation?

P. Boyer, 1988, Trends in biochemical sciences.

Exchange of oxygen between phosphate and water catalyzed by the plasma membrane ATPase from the yeast Schizosaccharomyces pombe.

A. Goffeau, P. Boyer, D. McIntosh, 1982, The Journal of biological chemistry.

Contribution of 18O technology to the mechanism of the H+-ATPase from yeast plasma membrane.

A. Goffeau, P. Boyer, D. McIntosh, 1984, Current topics in cellular regulation.

The inhibition of the snooinoxidase system by α-tocopheryl phosphate and sodium dodecyl sulfate.

P. Boyer, M. Rabinovitz, 1950 .

Oxidative phosphorylation and photophosphorylation.

E. C. Slater, B Chance, B. Chance, 1977, Annual review of biochemistry.

Hydrolysis : peptide bonds

P. Boyer, 1971 .

Isotopic Probes of the Enolase Reaction Mechanism INITIAL AND EQUILIBRIUM ISOTOPE EXCHANGE RATES: PRIMARY AND SECONDARY ISOTOPE EFFECTS

P. Boyer, E. Dinovo, 1971 .

ROLE OF THE PHOSPHORYLATED IMIDAZOLE GROUP IN PHOSPHORYLATION AND ENERGY TRANSFER REACTIONS.

P. Boyer, R. Mitchell, G. Kreil, 1963, Federation proceedings.

The biological inactivity of glucose 6-phosphite, inorganic phosphites and other phosphites.

H. Robertson, P. Boyer, 1956, Archives of biochemistry and biophysics.

The mechanism of enzymic phosphate transfer reactions.

P. Boyer, A. Falcone, W. Harrison, 1955, The Journal of biological chemistry.

Kinetic analysis of enzyme reactions. I. Further considerations of enzyme inhibition and analysis of enzyme activation.

P. Boyer, H. Segal, J. Kachmar, 1952, Enzymologia.

[14] Succinyl coenzyme a synthetase from Escherichia coli: [EC 6.2.1.5 Succinate: CoA ligase (SDP)]

P. Boyer, W. A. Bridger, R. Ramaley, 1969 .

Initial formation of ATP in photophosphorylation does not require a proton gradient

P. Boyer, M. Avron, C. Vinkler, 1978 .

Effect of temperature and antioxidants upon the lipoxidase-catalyzed oxidation of sodium linoleate.

P. Boyer, A. Tappel, W. O. Lundberg, 1953, Archives of biochemistry and biophysics.

Orthophosphite as a buffer for biological studies.

H. Robertson, P. Boyer, 1956, Archives of biochemistry and biophysics.

Mechanism of enzyme action.

P. Boyer, 1960, Annual review of biochemistry.

Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation.

P. Boyer, M. Deluca, K. Ebner, 1962, The Journal of biological chemistry.

Rapid transfer of oxygens from inorganic phosphate to glutamine catalyzed by Escherichia coli glutamine synthetase.

P. Boyer, B. O. Stokes, 1976, The Journal of biological chemistry.

Substrate binding and reaction intermediates of glutamine synthetase (Escherichia coli W) as studied by isotope exchanges.

P. Boyer, F. Wedler, 1972, The Journal of biological chemistry.

Some chemical characteristics of dimethylsuberimidate and its effect on sarcoplasmic reticulum vesicles.

P. Boyer, Y. Yuthavong, N. Feldman, 1975, Biochimica et biophysica acta.

32P-labeling of mitochondrial protein and lipid fractions and their relation to oxidative phosphorylation.

P. Boyer, L. Bieber, 1966, The Journal of biological chemistry.

Evaluation of the partitioning of bound inorganic phosphate during medium and intermediate phosphate in equilibrium water oxygen exchange reactions of yeast inorganic pyrophosphatase.

P. Boyer, D. Hackney, 1978, Proceedings of the National Academy of Sciences of the United States of America.

[10] The application of 18O methods to oxidative phosphorylation

P. Boyer, D. M. Bryan, 1967 .

The combination of fatty acids and related compounds with serum albumin; the nature and extent of the combination.

P. Boyer, J. M. Luck, G. A. Ballou, 1947, The Journal of biological chemistry.

The incorporation of p-fluorophenylalanine into some rabbit enzymes and other proteins.

P. Boyer, E. Westhead, 1961, Biochimica et biophysica acta.

The lack of incorporation of canavanine into rabbit-muscle protein in vivo.

P. Boyer, D. Graves, R. Boldt, 1962, Biochimica et biophysica acta.

Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site.

P. Boyer, R. L. Cross, Z. Xue, 1987, Proceedings of the National Academy of Sciences of the United States of America.

CHARACTERIZATION OF ACYL PHOSPHATE IN TRANSPORT ATPases BY A BOROHYDRIDE REDUCTION METHOD *

P. Boyer, C. Degani, A. Dahms, 1974, Annals of the New York Academy of Sciences.

The correlation of reaction kinetics and substrate binding with the mechanism of pyruvate kinase.

L. F. Hass, P. Boyer, A. Reynard, 1961, The Journal of biological chemistry.

Relationships of pH to exchange rates and deuterium isotope effects in the fumarase reaction

P. Boyer, E. Dinovo, K. Berman, 1971 .

Catalytic site occupancy during ATP synthase catalysis

P. Boyer, Paul D Boyer, 2002, FEBS letters.

Initial and equilibrium 18O, 14C, 3H, and 2H exchange rates as probes of the fumarase reaction mechanism.

P. Boyer, P D Boyer, J N Hansen, 1969, The Journal of biological chemistry.

Source of the oxygen in the C-O-P linkage of the acyl phosphate in transport adenosine triphosphatases.

P. Boyer, A. Dahms, T. Kanazawa, 1973, The Journal of biological chemistry.

Occurrence and characteristics of a rapid exchange of phosphate oxygens catalyzed by sarcoplasmic reticulum vesicles.

P. Boyer, T. Kanazawa, 1973, The Journal of biological chemistry.

The combination of fatty acids and related compounds with serum albumin; stabilization against urea and guanidine denaturation.

P. Boyer, J. M. Luck, G. A. Ballou, 1946, The Journal of biological chemistry.

Reconstituted mitochondrial oligomycin‐sensitive ATPase (F0F1) with intermediate Pi ⇌ HOH exchange but no Pi ⇌ ATP exchange activity

P. Boyer, C. Carlsson, L. Ernster, 1977 .

Protein-bound sulfhydryl groups and thiolesters in mitochondria and submitochondrial particles and their relationships to oxidative phosphorylation.

P. Boyer, O. Chude, 1974, Archives of biochemistry and biophysics.

The reversal of the myosin and actomyosin ATPase reactions and the free energy of ATP binding to myosin.

P. Boyer, R. G. Wolcott, 1974, Biochemical and biophysical research communications.

Demonstration of a transitory tight binding of ATP and of committed P(i) and ADP during ATP synthesis by chloroplasts.

P. Boyer, D. J. Smith, 1976, Proceedings of the National Academy of Sciences of the United States of America.

Light-driven ATP formation from 32Pi by chloroplast thylakoids without detectable labeling of ADP, as measured by rapid mixing and acid quench techniques.

P. Boyer, G. Rosen, C. Vinkler, 1978, The Journal of biological chemistry.

A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions.

P. Boyer, R. L. Cross, W. Momsen, 1973, Proceedings of the National Academy of Sciences of the United States of America.

Chloroplast F1 ATPase has more than three nucleotide binding sites, and 2-azido-ADP or 2-azido-ATP at both catalytic and noncatalytic sites labels the beta subunit.

R L Cross, P. Boyer, R. L. Cross, 1987, Biochemistry.

Kinetic characteristics of the acetylation of isoniazid and p-aminosalicylic acid by a liver-enzyme preparation.

P. Boyer, J. Jenne, 1962, Biochimica et biophysica acta.

The activation by K+ and occurrence of pyruvic phosphoferase in different species.

P. Boyer, 1953, Journal of cellular and comparative physiology.

Characterization of sarcoplasmic reticulum adenosinetriphosphatase purified by selective column adsorption.

P. Boyer, A. Gafni, 1984, Biochemistry.

Evidence for detection of AT32P bound at the coupling sites of mitochondrial oxidative phosphorylation

P. Boyer, R. L. Cross, 1973 .

Rates of various reactions catalyzed by ATP synthase as related to the mechanism of ATP synthesis.

K F LaNoue, P. Boyer, K. Lanoue, 1991, The Journal of biological chemistry.

Catalytic properties of the ATPase on submitochondrial particles after exchange of tightly bound nucleotides under different steady state conditions

P. Boyer, J. A. Myers, 1983, FEBS letters.

ATP AND ADP MODULATIONS OF CATALYSIS BY F1 AND Ca2, Mg2+‐ATPases *

P. Boyer, L. T. Smith, W. Kohlbrenner, 1982, Annals of the New York Academy of Sciences.

The mechanism of stimulation of MgATPase activity of chloroplast F1-ATPase by non-catalytic adenine-nucleotide binding. Acceleration of the ATP-dependent release of inhibitory ADP from a catalytic site.

P. Boyer, M. Murataliev, 1992, European journal of biochemistry.

The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic site.

P. Boyer, Y. Milgrom, 1990, Biochimica et biophysica acta.

Characteristics of the combination of inhibitory Mg2+ and azide with the F1 ATPase from chloroplasts.

P. Boyer, Y. Milgrom, M. Murataliev, 1991, Biochemistry.

The role of tightly bound ADP on chloroplast ATPase.

P. Boyer, R. I. Feldman, 1985, The Journal of biological chemistry.

[117] 32P-labeling of mitochondrial protein and lipid fractions

P. Boyer, L. Bieber, 1967 .

CHEMICAL, CLINICAL, AND IMMUNOLOGICAL STUDIES ON THE PRODUCTS OF HUMAN PLASMA FRACTIONATION. V. THE INFLUENCE OF NON-POLAR ANIONS ON THE THERMAL STABILITY OF SERUM ALBUMIN.

P. Boyer, J. M. Luck, G. A. Ballou, 1944, The Journal of clinical investigation.

Energy, Life, and ATP (Nobel Lecture).

P. Boyer, Paul D Boyer, 1998, Angewandte Chemie.

Use of 14C-carboxyl-luciferin in determining the mechanism of the firefly luciferase catalyzed reactions.

P. Boyer, M. Deluca, J. Wannlund, 1978, Biochemical and biophysical research communications.

Dephosphorylation of succinyl coenzyme A synthetase as related to enzyme specificity and catalytic intermediates.

P. Boyer, J. Robinson, R. W. Benson, 1969, Biochemistry.

The formation and reactions of a nonphosphorylated high energy form of succinyl coenzyme A synthetase.

P. Boyer, L. Butler, R. Ramaley, 1967, The Journal of biological chemistry.

The association of readily-soluble bound phosphohistidine from mitochondria with succinate thiokinase.

P. Boyer, R. Mitchell, L. Butler, 1964, Biochemical and biophysical research communications.

Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model.

P. Boyer, M. Gresser, J. A. Myers, 1982, The Journal of biological chemistry.

Direct and 18-O-exchange measurements relevant to possible activated or phosphorylated states of myosin.

H. Fromm, P. Boyer, L. Sartorelli, 1966, Biochemistry.

Guanosine and formycin triphosphates bind at non‐catalytic nucleotide binding sites of CF1 ATPase and inhibit ATP hydrolysis

P. Boyer, K. Guerrero, L. Ehler, 1990, FEBS letters.

From Human Serum Albumin to Rotational Catalysis by ATP Synthase

P. Boyer, 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

On the enzymic synthesis of lactose-1-PO4.

P. Boyer, J. Gander, W. Petersen, 1957, Archives of biochemistry and biophysics.

On the mechanism of sulfite activation of chloroplast thylakoid ATPase and the relation of ADP tightly bound at a catalytic site to the binding change mechanism.

P. Boyer, Z. Du, 1990, Biochemistry.

Medium ADP and not ADP already tightly bound to phylakoid membranes forms the initial ATP in chloroplast phosphorylation.

P. Boyer, J. Rosing, D. J. Smith, 1976, Biochemical and biophysical research communications.

Catalytic properties of the F1-adenosine triphosphatase from Escherichia coli K-12 and its genetic variants as revealed by 18O exchanges.

P. Boyer, A. E. Senior, J. M. Wood, 1987, The Journal of biological chemistry.

Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase.

P. Boyer, P D Boyer, R. Hutton, 1979, The Journal of biological chemistry.

Characteristics of the reversible heat, solvent, and detergent denaturation of leucine binding protein.

P. Boyer, K. Berman, 1972, Biochemistry.

The Preparation of a Reversible Oxidation Product of α-Tocopherol, α-Tocopheroxide and of Related Oxides1

P. Boyer, 1951 .

Sarcoplasmic reticulum adenosinetriphosphatase phosphorylation from inorganic phosphate. Theoretical and experimental reinvestigation.

P. Boyer, P. Champeil, F. Guillain, 1984, Biochemistry.

Adenosine 5'-triphosphate modulation of catalytic intermediates of calcium ion activated adenosinetriphosphatase of sarcoplasmic reticulum subsequent to enzyme phosphorylation.

P. Boyer, D. Mcintosh, 1983, Biochemistry.

Characterization of medium inorganic phosphate-water exchange catalyzed by sarcoplasmic reticulum vesicles.

P. Boyer, M. Ariki, 1980, Biochemistry.

Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzyme.

P. Boyer, V. Kasho, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Toward an Adequate Scheme for the ATP Synthase Catalysis

P. Boyer, 2001, Biochemistry (Moscow).

A Research Journey with ATP Synthase

P. Boyer, Paul D Boyer, 2002, The Journal of Biological Chemistry.

Molecular motors: What makes ATP synthase spin?

P. Boyer, Paul D. Boyer, 1999, Nature.

ATP synthase--past and future.

P. Boyer, 1998, Biochimica et biophysica acta.

The apparent absolute requirement of adenosine diphosphate for the inorganic phosphate--water exchange of oxidative phosphorylation.

P. Boyer, D. H. Jones, 1969, The Journal of biological chemistry.

Mechanistic implications of Mg++, adenine nucleotide, and inhibitor effects on energy-linked reactions of submitochondrial particles.

P. Boyer, R. Mitchell, R. D. Hill, 1967, The Journal of biological chemistry.

Occurrence and possible mechanism of 32P and 18O exchange reactions of photophosphorylation.

P. Boyer, N. Shavit, G. Skye, 1967, The Journal of biological chemistry.

The catalysis by modified chloroplasts of the Pi-ATP, Pi-HOH and ATP-HOH exchange reactions in the absence of light.

P. Boyer, N. Shavit, G. Skye, 1967, Biochemical and biophysical research communications.

Source of oxygen in adenosine triphosphate formed by illumination or by acid-base transition of chloroplasts.

P. Boyer, N. Shavit, 1966, The Journal of biological chemistry.

An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitions.

P. Boyer, J. Rosing, C. Kayalar, 1977, The Journal of biological chemistry.

Characteristics of the chloroplast ATP synthase as revealed by reaction at low ADP concentrations

P. Boyer, Paul D. Boyer, Steven D. Stroop, 1985 .

Direct Oxygen Transfer in Enzymic Syntheses Coupled to Adenosine Triphosphate Degradation1

P. Boyer, W. W. Luchsinger, O. J. Koeppe, 1956 .

CHARACTERISTICS OF AN ORTHOPHOSPHATE OXYGEN EXCHANGE CATALYZED BY MYOSIN, ACTOMYOSIN, AND MUSCLE FIBERS.

P. Boyer, E. Benson, M. Dempsey, 1963, The Journal of biological chemistry.

Chemical structure in relation to vitamin E function.

P. Boyer, M. Rabinovitz, E. Liebe, 1951, Journal of Biological Chemistry.

The fate of oxygens of inorganic phosphate in photophosphorylation.

P. Boyer, A. Schulz, 1961, Archives of biochemistry and biophysics.

IV. 1 – SOME ASPECTS OF PROTEIN STRUCTURE IN RELATION TO THE ROLE OF —SH AND —S—S— GROUPS IN ENZYMIC CATALYSIS*

P. Boyer, A. Schulz, 1959 .

THE LIGHT-INDUCED FORMATION OF RAPIDLY PHOSPHORYLATED COMPOUNDS IN CHLOROPLASTS.

P. Boyer, J. W. Hinkson, 1965, Archives of biochemistry and biophysics.

The enzymes. Hydrolysis: peptide bonds. 3rd edition. Vol. 3.

P. Boyer, 1970 .

Derivatization of the catalytic subunits of the chloroplast ATPase by 2-azido-ATP and dicyclohexylcarbodiimide. Evidence for catalytically induced interchange of the subunits.

P. Boyer, T. Mélèse, 1985, The Journal of biological chemistry.

THE PAPAIN DIGESTION OF NATIVE, DENATURED, AND "STABILIZED" HUMAN SERUM ALBUMIN

P. Boyer, J. M. Luck, R. Rice, 1945 .

Subunit interaction during catalysis: alternating site cooperativity in photophosphorylation shown by substrate modulation of [18O]ATP species formation.

P. Boyer, D. Hackney, G. Rosen, 1979, Proceedings of the National Academy of Sciences of the United States of America.

Patterns of oxygen interchange between water, substrates, and phosphate compounds of Escherichia coli and Bacillus subtilis.

P. Boyer, S. Chaney, J. Duffy, 1972, Journal of Biological Chemistry.

Hydrolysis : other C-N bonds phosphate esters

P. Boyer, 1971 .

MgADP and free Pi as the substrates and the Mg2+ requirement for photophosphorylation.

P. Boyer, J. M. Zhou, 1992, Biochemistry.

The rate of release of ATP from its complex with myosin.

P. Boyer, J. Cardon, 1978, European journal of biochemistry.

Catalysis of an inorganic phosphate-H2-O-18 exchange by actomysin and myosin.

P. Boyer, M. Dempsey, 1961, The Journal of biological chemistry.

Studies on possible phosphoryl enzyme formation in catalysis by hexokinase, pyruvate kinase, and glucose 6-phosphatase.

L. F. Hass, P. Boyer, A. Reynard, 1961, The Journal of biological chemistry.

Modulation of the GTPase activity of the chloroplast F1-ATPase by ATP binding at noncatalytic sites.

P. Boyer, Z. Xue, 1989, European journal of biochemistry.

Evidence that energization of the chloroplast ATP synthase favors ATP formation at the tight binding catalytic site and increases the affinity for ADP at another catalytic site.

P. Boyer, J. M. Zhou, 1993, The Journal of biological chemistry.

EQUILIBRIUM AND NET REACTION RATES IN RELATION TO THE MECHANISM OF YEAST HEXOKINASE.

H. Fromm, P. Boyer, E. Silverstein, 1964, The Journal of biological chemistry.

BINDING SITES, REACTIVATION PHENOMENA, AND POSSIBLE -S-S- GROUPS OF RABBIT MUSCLE ALDOLASE.

P. Boyer, L. Butler, E. Westhead, 1963, Biochemistry.

The effect of azide on phosphorylation accompanying electron transport and glycolysis.

H. Robertson, P. Boyer, 1955, Journal of Biological Chemistry.

F1 ATPase from the thermophilic bacterium PS3 (TF1) shows ATP modulation of oxygen exchange.

P. Boyer, M. Yoshida, V. Kasho, 1989, Biochemistry.

Catalytic and Noncatalytic Nucleotide Binding Sites of F1-ATPases: Probes of Location, Structure and Function by Use of 2-N3-ATP

P. Boyer, R. L. Cross, Z. Xue, 1989 .

Interaction of mitochondrial F1-ATPase with trinitrophenyl derivatives of ATP and ADP. Participation of third catalytic site and role of Mg2+ in enzyme inactivation.

P. Boyer, M. Murataliev, 1994, The Journal of biological chemistry.

OXYGEN EXCHANGES CATALYZED BY AND THE MECHANISM OF ACYL PHOSPHATE FORMATION IN TRANSPORT ATPases

P. Boyer, A. Stephen Dahms, 1974, Annals of the New York Academy of Sciences.

Characteristics of the formation of enzyme-bound ATP from medium inorganic phosphate by mitochondrial F1 adenosinetriphosphatase in the presence of dimethyl sulfoxide.

P. Boyer, R. Kandpal, K. Stempel, 1987, Biochemistry.

Catalytic properties of beef heart mitochondrial ATPase modified with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Evidence for catalytic site cooperativity during ATP synthesis.

P. Boyer, W. Kohlbrenner, 1982, The Journal of biological chemistry.

Rate and Extent of Labelling of Bound Phosphohistidine as Related to its Role in Mitochondria

P. Boyer, L. Bieber, O. Lindberg, 1964, Nature.

Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase Amino acid sequences of β‐subunit tryptic peptides labeled with 2‐azido‐ATP

P. Boyer, B. Hicke, J. Wise, 1987, FEBS letters.

Response of an unidentified phosphate fraction and of bound phosphohistidine in mitochondria to Ca++, uncouplers, and inhibitors

P. Boyer, A. Norman, O. Lindberg, 1964 .

Studies concerning the mechanism of action of acetoacetyl succinic thiophorase by use of O18.

P. Boyer, A. Falcone, 1959, Archives of biochemistry and biophysics.

The combination of fatty acids and related compounds with serum albumin; stabilization against heat denaturation.

P. Boyer, F. G. Lum, 1946, The Journal of biological chemistry.

CHEMICAL MECHANISM OF SONIC, ACID, ALKALINE AND ENZYMIC DEGRADATION OF DNA.

P. Boyer, O. Richards, P. Boyer, 1965, Journal of molecular biology.

Modulation of stoichiometry of the sarcoplasmic reticulum calcium pump may enhance thermodynamic efficiency.

P. Boyer, A. Gafni, 1985, Proceedings of the National Academy of Sciences of the United States of America.

CHEMICAL AND BIOLOGICAL STUDIES RELATED TO THE METABOLIC FUNCTION OF VITAMIN E

P. Boyer, M. Rabinovitz, E. Liebe, 1949 .

The equivalence of phosphate oxygens for exchange and the hydrolysis characteristics revealed by the distribution of [18O]Pi species formed by myosin and actomyosin ATPase.

P. Boyer, D. Hackney, J. Sleep, 1980, The Journal of biological chemistry.

Combinations of modified serum γ-globulin with other proteins

P. Boyer, E. Turner, 1952 .

An assessment of the exchangeability of water molecules in the interior of chymotrypsinogen in solution.

P. Boyer, B. Weber, M. Storm, 1974, Archives of biochemistry and biophysics.

[27] Rapid nucleotide labeling and 18O exchange probes of intermediate states in electron-transport-coupled phosphorylation1☆

P. Boyer, K. Stempel, 1979 .

Assessment of the rate of bound substrate interconversion and of ATP acceleration of product release during catalysis by mitochondrial adenosine triphosphatase.

P. Boyer, C. C. O'neal, 1984, The Journal of biological chemistry.