- 1997 Nobel Laureate in Chemistry
- Marlow Medal, Faraday Society
- Langmuir Award
- Harrison Howe Award
- G. N. Lewis Award
- Morley Award
- Pauling Award
- Award for Computers in Chemistry, American Chemical Society
- U.S. Senior Scientist Award, Humboldt Foundation
- Wheland Award, University of Chicago
- Evans Award, Ohio State University
- Oesper Award, University of Cincinnati
- Davy Medal, Royal Society, U.K.
- Wolf Prize
1. Boyer Paul D A research journey with ATP synthase. The Journal of biological chemistry 2002;277(42):39045-61.
2. Boyer Paul D Catalytic site occupancy during ATP synthase catalysis. FEBS letters 2002;512(1-3):29-32.
3. Boyer P D. Toward an adequate scheme for the ATP synthase catalysis. Biochemistry. Biokhimii?a 2001;66(10):1058-66.
4. Boyer P D. New insights into one of nature’s remarkable catalysts, the ATP synthase. Molecular cell 2001;8(2):246-7.
5. Boyer P D. Catalytic site forms and controls in ATP synthase catalysis. Biochimica et biophysica acta 2000;1458(2-3):252-62.
6. Boyer P D. What makes ATP synthase spin? Nature 1999;402(6759):247, 249.
7. Boyer P D. ATP synthase–past and future. Biochimica et biophysica acta 1998;1365(1-2):3-9.
8. Boyer P D. Energy, life, and ATP. Bioscience reports 1998;18(3):97-117.
9. Milgrom Y M; Murataliev M B; Boyer P D. Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase. The Biochemical journal 1998;330 ( Pt 2)():1037-43.
10. Boyer P D. The ATP synthase–a splendid molecular machine. Annual review of biochemistry 1997;66():717-49.
11. Boyer P D. From human serum albumin to rotational catalysis by ATP synthase. The FASEB journal : official publication of the Federation of American Societies for Experimental Biology 1995;9(7):559-61.
12. Jaskoll T; Boyer P D.; Melnick M Tumor necrosis factor-alpha and embryonic mouse lung morphogenesis. Developmental dynamics : an official publication of the American Association of Anatomists 1994;201(2):137-50.
13. Murataliev M B; Boyer P D. Interaction of mitochondrial F1-ATPase with trinitrophenyl derivatives of ATP and ADP. Participation of third catalytic site and role of Mg2+ in enzyme inactivation. The Journal of biological chemistry 1994;269(22):15431-9.
14. Zhou J M; Boyer P D. 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. The Journal of biological chemistry 1993;268(3):1531-8.
15. Boyer P D. The binding change mechanism for ATP synthase–some probabilities and possibilities. Biochimica et biophysica acta 1993;1140(3):215-50.
16. Kasho V N; Allison W S; Boyer P D. Study of the mechanism of MF1 ATPase inhibition by fluorosulfonylbenzoyl inosine, quinacrine mustard, and efrapeptin using intermediate 18O exchange as a probe. Archives of biochemistry and biophysics 1993;300(1):293-301.
17. Murataliev M B; Boyer P D. 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. European journal of biochemistry / FEBS 1992;209(2):681-7.
18. Zhou J M; Boyer P D. MgADP and free Pi as the substrates and the Mg2+ requirement for photophosphorylation. Biochemistry 1992;31(12):3166-71.
19. Murataliev M B; Milgrom Y M; Boyer P D. Characteristics of the combination of inhibitory Mg2+ and azide with the F1 ATPase from chloroplasts. Biochemistry 1991;30(34):8305-10.
20. Milgrom Y M; Ehler L L; Boyer P D. The characteristics and effect on catalysis of nucleotide binding to noncatalytic sites of chloroplast F1-ATPase. The Journal of biological chemistry 1991;266(18):11551-8.
21. Berkich D A; Williams G D; Masiakos P T; Smith M B; Boyer P D.; LaNoue K F Rates of various reactions catalyzed by ATP synthase as related to the mechanism of ATP synthesis. The Journal of biological chemistry 1991;266(1):123-9.
22. Milgrom Y M; Ehler L L; Boyer P D. ATP binding at noncatalytic sites of soluble chloroplast F1-ATPase is required for expression of the enzyme activity. The Journal of biological chemistry 1990;265(31):18725-8.
23. Milgrom Y M; Boyer P D. The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic site. Biochimica et biophysica acta 1990;1020(1):43-8.
24. Guerrero K J; Xue Z X; Boyer P D. 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. The Journal of biological chemistry 1990;265(27):16280-7.
25. Guerrero K J; Ehler L L; Boyer P D. Guanosine and formycin triphosphates bind at non-catalytic nucleotide binding sites of CF1 ATPase and inhibit ATP hydrolysis. FEBS letters 1990;270(1-2):187-90.
26. Du Z Y; Boyer P D. 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. Biochemistry 1990;29(2):402-7.
27. Kasho V N; Boyer P D. Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzyme. Proceedings of the National Academy of Sciences of the United States of America 1989;86(22):8708-11.
28. Kasho V N; Yoshida M; Boyer P D. F1 ATPase from the thermophilic bacterium PS3 (TF1) shows ATP modulation of oxygen exchange. Biochemistry 1989;28(17):6949-54.
29. Boyer P D. A perspective of the binding change mechanism for ATP synthesis. The FASEB journal : official publication of the Federation of American Societies for Experimental Biology 1989;3(10):2164-78.
30. Boyer P D.; Diamond R A; Rothenberg E V Changes in inducibility of IL-2 receptor alpha-chain and T cell-receptor expression during thymocyte differentiation in the mouse. Journal of immunology (Baltimore, Md. : 1950) 1989;142(12):4121-30.
31. Xue Z; Boyer P D. Modulation of the GTPase activity of the chloroplast F1-ATPase by ATP binding at noncatalytic sites. European journal of biochemistry / FEBS 1989;179(3):677-81.
32. Xue Z X; Melese T; Stempel K E; Reedy T J; Boyer P D. Properties of chloroplast F1-ATPase partially modified by 2-azido adenine nucleotides, including demonstration of three catalytic pathways. The Journal of biological chemistry 1988;263(32):16880-5.
33. Guerrero K J; Boyer P D. 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. Biochemical and biophysical research communications 1988;154(3):854-60.
34. Rothenberg E V; McGuire K L; Boyer P D. Molecular indices of functional competence in developing T cells. Immunological reviews 1988;104():29-53.
35. Zhou J M; Xue Z X; Du Z Y; Melese T; Boyer P D. Relationship of tightly bound ADP and ATP to control and catalysis by chloroplast ATP synthase. Biochemistry 1988;27(14):5129-35.
36. Boyer P D.; Rothenberg E V IL-2 receptor inducibility is blocked in cortical-type thymocytes. Journal of immunology (Baltimore, Md. : 1950) 1988;140(9):2886-92.
37. Melese T; Xue Z X; Stempel K E; Boyer P D. Catalytic properties of chloroplast F1-ATPase modified at catalytic or noncatalytic sites by 2-azido adenine nucleotides. The Journal of biological chemistry 1988;263(12):5833-40.
38. Baldarelli R M; Mahoney P A; Salas F; Gustavson E; Boyer P D.; Chang M F; Roark M; Lengyel J A Transcripts of the Drosophila blastoderm-specific locus, terminus, are concentrated posteriorly and encode a potential DNA-binding finger. Developmental biology 1988;125(1):85-95.
39. Boyer P D. Bioenergetic coupling to protonmotive force: should we be considering hydronium ion coordination and not group protonation? Trends in biochemical sciences 1988;13(1):5-7.
40. Boyer P D. The unusual enzymology of ATP synthase. Biochemistry 1987;26(26):8503-7.
41. Wise J G; Hicke B J; Boyer P D. Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase. Amino acid sequences of beta-subunit tryptic peptides labeled with 2-azido-ATP. FEBS letters 1987;223(2):395-401.
42. Xue Z X; Miller C G; Zhou J M; Boyer P D. Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase. Photoaffinity labeling and peptide sequencing. FEBS letters 1987;223(2):391-4.
43. Cross R L; Cunningham D; Miller C G; Xue Z X; Zhou J M; Boyer P D. 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. Proceedings of the National Academy of Sciences of the United States of America 1987;84(16):5715-9.
44. Xue Z X; Zhou J M; Melese T; Cross R L; Boyer P D. 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. Biochemistry 1987;26(13):3749-53.
45. Kandpal R P; Stempel K E; Boyer P D. Characteristics of the formation of enzyme-bound ATP from medium inorganic phosphate by mitochondrial F1 adenosinetriphosphatase in the presence of dimethyl sulfoxide. Biochemistry 1987;26(6):1512-7.
46. Boyer P D.; Mahoney P A; Lengyel J A Molecular characterization of bsg25D: a blastoderm-specific locus of Drosophila melanogaster. Nucleic acids research 1987;15(5):2309-25.
47. Stroop S D; Boyer P D. Catalytic and regulatory effects of light intensity on chloroplast ATP synthase. Biochemistry 1987;26(5):1479-84.
48. Wood J M; Wise J G; Senior A E; Futai M; Boyer P D. Catalytic properties of the F1-adenosine triphosphatase from Escherichia coli K-12 and its genetic variants as revealed by 18O exchanges. The Journal of biological chemistry 1987;262(5):2180-6.
49. Kandpal R P; Boyer P D. Escherichia coli F1 ATPase is reversibly inhibited by intra- and intersubunit crosslinking: an approach to assess rotational catalysis. Biochimica et biophysica acta 1987;890(1):97-105.
50. Boyer P D. A sensitive technique for detection of RNA with single-stranded probes. Nucleic acids research 1986;14(18):7505.
51. Boyer P D. The case for a return to fixed indirect costs. Science (New York, N.Y.) 1986;232(4757):1508-9.
52. Wu D; Boyer P D. 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+. Biochemistry 1986;25(11):3390-6.
53. Stempel K E; Boyer P D. Refinements in oxygen-18 methodology for the study of phosphorylation mechanisms. Methods in enzymology 1986;126():618-39.
54. Melese T; Boyer P D. Derivatization of the catalytic subunits of the chloroplast ATPase by 2-azido-ATP and dicyclohexylcarbodiimide. Evidence for catalytically induced interchange of the subunits. The Journal of biological chemistry 1985;260(29):15398-401.
55. Feldman R I; Boyer P D. The role of tightly bound ADP on chloroplast ATPase. The Journal of biological chemistry 1985;260(24):13088-94.
56. Kandpal R P; Melese T; Stroop S D; Boyer P D. Mitochondrial F1-ATPase will bind and cleave ATP but only slowly release ADP after N,N’-dicyclohexylcarbodiimide or 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole derivatization. The Journal of biological chemistry 1985;260(9):5542-7.
57. Gafni A; Boyer P D. Modulation of stoichiometry of the sarcoplasmic reticulum calcium pump may enhance thermodynamic efficiency. Proceedings of the National Academy of Sciences of the United States of America 1985;82(1):98-101.
58. Kasho V N; Boyer P D. Relationships of inosine triphosphate and bicarbonate effects on F1 ATPase to the binding change mechanism. Journal of bioenergetics and biomembranes 1984;16(5-6):407-19.
59. Guillain F; Champeil P; Boyer P D. Sarcoplasmic reticulum adenosinetriphosphatase phosphorylation from inorganic phosphate. Theoretical and experimental reinvestigation. Biochemistry 1984;23(20):4754-61.
60. Gafni A; Boyer P D. Characterization of sarcoplasmic reticulum adenosinetriphosphatase purified by selective column adsorption. Biochemistry 1984;23(19):4362-7.
61. O’Neal C C; Boyer P D. Assessment of the rate of bound substrate interconversion and of ATP acceleration of product release during catalysis by mitochondrial adenosine triphosphatase. The Journal of biological chemistry 1984;259(9):5761-7.
62. Amory A; Goffeau A; McIntosh D B; Boyer P Contribution of 18O technology to the mechanism of the H+-ATPase from yeast plasma membrane. Current topics in cellular regulation 1984;24():471-83.
63. Myers J A; Boyer P D. Catalytic properties of the ATPase on submitochondrial particles after exchange of tightly bound nucleotides under different steady state conditions. FEBS letters 1983;162(2):277-81.
64. Smith L T; Rosen G; Boyer P D. Properties of ATP tightly bound to catalytic sites of chloroplast ATP synthase. The Journal of biological chemistry 1983;258(18):10887-94.
65. Kohlbrenner W E; Boyer P D. Probes of catalytic site cooperativity during catalysis by the chloroplast adenosine triphosphate and the adenosine triphosphate synthase. The Journal of biological chemistry 1983;258(18):10881-6.
66. McIntosh D B; Boyer P D. Adenosine 5’-triphosphate modulation of catalytic intermediates of calcium ion activated adenosinetriphosphatase of sarcoplasmic reticulum subsequent to enzyme phosphorylation. Biochemistry 1983;22(12):2867-75.
67. Clarke C; Berenson J; Goverman J; Boyer P D.; Crews S; Siu G; Calame K An immunoglobulin promoter region is unaltered by DNA rearrangement and somatic mutation during B-cell development. Nucleic acids research 1982;10(23):7731-49.
68. Amory A; Goffeau A; McIntosh D B; Boyer P D. Exchange of oxygen between phosphate and water catalyzed by the plasma membrane ATPase from the yeast Schizosaccharomyces pombe. The Journal of biological chemistry 1982;257(21):12509-16.
69. Gresser M J; Myers J A; Boyer P D. 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. The Journal of biological chemistry 1982;257(20):12030-8.
70. Cardon J W; Boyer P D. Subunit interaction in catalysis. Some experimental and theoretical approaches with glyceraldehyde-3-phosphate dehydrogenase. The Journal of biological chemistry 1982;257(13):7615-22.
71. Kohlbrenner W E; Boyer P D. 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. The Journal of biological chemistry 1982;257(7):3441-6.
72. Guillain F P; Boyer P D. Correlation of intrinsic fluorescence and oxygen-exchange measurements of phosphorylation of sarcoplasmic reticulum ATPase from inorganic phosphate. Annals of the New York Academy of Sciences 1982;402():566-8.
73. Boyer P D.; Kohlbrenner W E; McIntosh D B; Smith L T; O’Neal C C ATP and ADP modulations of catalysis by F1 and Ca2+, Mg2+-ATPases. Annals of the New York Academy of Sciences 1982;402():65-83.
74. Bild G S; Boyer P D. Subunit interaction during catalysis: ammonium ion modulation of catalytic steps in the Escherichia coli glutamine synthetase reaction. Biochemistry 1980;19(25):5774-81.
75. Bild G S; Janson C A; Boyer P D. Subunit interaction during catalysis. ATP modulation of catalytic steps in the succinyl-CoA synthetase reaction. The Journal of biological chemistry 1980;255(17):8109-15.
76. Boyer P D.; Ariki M 18O-probes of phosphoenzyme formation and cooperativity with sarcoplasmic reticulum ATPase. Federation proceedings 1980;39(7):2410-4.
77. Sleep J A; Hackney D D; Boyer P D. 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. The Journal of biological chemistry 1980;255(9):4094-9.
78. Ariki M; Boyer P D. Characterization of medium inorganic phosphate-water exchange catalyzed by sarcoplasmic reticulum vesicles. Biochemistry 1980;19(9):2001-4.
79. Vinkler C; Avron M; Boyer P D. Effects of permeant buffers on the initial time course of photophosphorylation and postillumination phosphorylation. The Journal of biological chemistry 1980;255(6):2263-6.
80. Hackney D D; Stempel K E; Boyer P D. Oxygen-18 probes of enzymic reactions of phosphate compounds. Methods in enzymology 1980;64():60-83.
81. Rosen G; Gresser M; Vinkler C; Boyer P D. Assessment of total catalytic sites and the nature of bound nucleotide participation in photophosphorylation. The Journal of biological chemistry 1979;254(21):10654-61.
82. Gresser M; Cardon J; Rosen G; Boyer P D. Demonstration and quantitation of catalytic and noncatalytic bound ATP in submitochondrial particles during oxidative phosphorylation. The Journal of biological chemistry 1979;254(21):10649-53.
83. Hutton R L; Boyer P D. Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase. The Journal of biological chemistry 1979;254(20):9990-3.
84. Hackney D D; Rosen G; Boyer P D. Subunit interaction during catalysis: alternating site cooperativity in photophosphorylation shown by substrate modulation of [18O]ATP species formation. Proceedings of the National Academy of Sciences of the United States of America 1979;76(8):3646-50.
85. Janson C A; Degani C; Boyer P D. The formation of enzyme-bound and medium pyrophosphate and the molecular basis of the oxygen exchange reaction of yeast inorganic pyrophosphatase. The Journal of biological chemistry 1979;254(10):3743-9.
86. Choate G L; Hutton R L; Boyer P D. Occurrence and significance of oxygen exchange reactions catalyzed by mitochondrial adenosine triphosphatase preparations. The Journal of biological chemistry 1979;254(2):286-90.
87. Boyer P D.; Stempel K Rapid nucleotide labeling and 18O exchange probes of intermediate states in electron-transport-coupled phosphorylation. Methods in enzymology 1979;55():245-61.
88. Sleep J A; Boyer P D. Effect of actin concentration on the intermediate oxygen exchange of myosin; relation to the refractory state and the mechanism of exchange. Biochemistry 1978;17(25):5417-22.
89. Cardon J W; Boyer P D. The rate of release of ATP from its complex with myosin. European journal of biochemistry / FEBS 1978;92(2):443-8.
90. Sleep J A; Hackney D D; Boyer P D. Characterization of phosphate oxygen exchange reactions catalyzed by myosin through measurement of the distribution of 18-O-labeled species. The Journal of biological chemistry 1978;253(15):5235-8.
91. Hackney D D; Boyer P D. Evaluation of the partitioning of bound inorganic phosphate during medium and intermediate phosphate in equilibrium water oxygen exchange reactions of yeast inorganic pyrophosphatase. Proceedings of the National Academy of Sciences of the United States of America 1978;75(7):3133-7.
92. Hackney D D; Boyer P D. Subunit interaction during catalysis. Implications of concentration dependency of oxygen exchanges accompanying oxidative phosphorylation for alternating site cooperativity. The Journal of biological chemistry 1978;253(9):3164-70.
93. Vinkler C; Rosen G; Boyer P D. Light-driven ATP formation from 32Pi by chloroplast thylakoids without detectable labeling of ADP, as measured by rapid mixing and acid quench techniques. The Journal of biological chemistry 1978;253(8):2507-10.
94. Wannlund J; DeLuca M; Stempel K; Boyer P D. Use of 14C-carboxyl-luciferin in determining the mechanism of the firefly luciferase catalyzed reactions. Biochemical and biophysical research communications 1978;81(3):987-92.
95. Hart R C; Stempel K E; Boyer P D.; Cormier M J Mechanism of the enzyme-catalyzed bioluminescent oxidation of coelenterate-type luciferin. Biochemical and biophysical research communications 1978;81(3):980-6.
96. Strayer D R; Boyer P D. Integrity of parental DNA during replication. Journal of molecular biology 1978;120(2):281-95.
97. de Meis L; Boyer P D. Induction by nucleotide triphosphate hydrolysis of a form of sarcoplasmic reticulum ATPase capable of medium phosphate-oxygen exchange in presence of calcium. The Journal of biological chemistry 1978;253(5):1556-9.
98. Ernster L; Carlsson C; Boyer P D. Reconstituted mitochondrial oligomycin-sensitive ATPase (F0F1) with intermediate Pi in equilibrium HOH exchange but no Pi in equilibrium ATP exchange activity. FEBS letters 1977;84(2):283-6.
99. Kayalar C; Rosing J; Boyer P D. An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitions. The Journal of biological chemistry 1977;252(8):2486-91.
100. Rosing J; Kayalar C; Boyer P D. Evidence for energy-dependent change in phosphate binding for mitochondrial oxidative phosphorylation based on measurements of medium and intermediate phosphate-water exchanges. The Journal of biological chemistry 1977;252(8):2478-85.
101. Tsuji F I; DeLuca M; Boyer P D.; Endo S; Akutagawa M Mechanism of the enzyme–catalyzed oxidation of Cypridina and firefly luciferins studied by means of 17O2 and H218O1. Biochemical and biophysical research communications 1977;74(2):606-13.
102. Boyer P D.; de Meis L; da Gloria Costa Carvalho M; Hackney D D Dynamic reversal of enzyme carboxyl group phosphorylation as the basis of the oxygen exchange catalyzed by sarcoplasmic reticulum adenosine triphosphatase. Biochemistry 1977;16(1):136-40.
103. Smith D J; Boyer P D. Demonstration of a transitory tight binding of ATP and of committed P(i) and ADP D.uring ATP synthesis by chloroplasts. Proceedings of the National Academy of Sciences of the United States of America 1976;73(12):4314-8.
104. Kayalar C; Rosing J; Boyer P D. 2,4-Dinitrophenol causes a marked increase in the apparent Km of Pi and of ADP for oxidative phosphorylation. Biochemical and biophysical research communications 1976;72(3):1153-9.
105. Rogers G A; Shaltiel N; Boyer P D. Facile alkylation of methionine by benzyl bromide and demonstration of fumarase inactivation accompanied by alkylation of a methionine residue. The Journal of biological chemistry 1976;251(18):5711-7.
106. Stokes B O; Boyer P D. Rapid transfer of oxygens from inorganic phosphate to glutamine catalyzed by Escherichia coli glutamine synthetase. The Journal of biological chemistry 1976;251(18):5558-64.
107. Rosing J; Smith D J; Kayalar C; Boyer P D. Medium ADP and not ADP already tightly bound to phylakoid membranes forms the initial ATP in chloroplast phosphorylation. Biochemical and biophysical research communications 1976;72(1):1-8.
108. Smith D J; Stokes B O; Boyer P D. Probes of initial phosphorylation events in ATP synthesis by chloroplasts. The Journal of biological chemistry 1976;251(14):4165-71.
109. Boyer P D. A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport. FEBS letters 1975;58(1):1-6.
110. Bagshaw C R; Trentham D R; Wolcott R G; Boyer P D. Oxygen exchange in the gamma-phosphoryl group of protein-bound ATP D.uring Mg2+-dependent adenosine triphosphatase activity of myosin. Proceedings of the National Academy of Sciences of the United States of America 1975;72(7):2592-6.
111. Boyer P D.; Stokes B O; Wolcott R G; Degani C Coupling of ”high-energy” phosphate bonds to energy transductions. Federation proceedings 1975;34(8):1711-7.
112. Yuthavong Y; Feldman N; Boyer P D. Some chemical characteristics of dimethylsuberimidate and its effect on sarcoplasmic reticulum vesicles. Biochimica et biophysica acta 1975;382(1):116-24.
113. Boyer P D. Energy transduction and proton translocation by adenosine triphosphatases. FEBS letters 1975;50(2):91-4.
114. Cross R L; Boyer P D. 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. Biochemistry 1975;14(2):392-8.
115. Wolcott R G; Boyer P D. Isotopic probes of catalytic steps of myosin adenosine triphosphatase. Journal of supramolecular structure 1975;3(2):154-61.
116. Weber B H; Storm M C; Boyer P D. An assessment of the exchangeability of water molecules in the interior of chymotrypsinogen in solution. Archives of biochemistry and biophysics 1974;163(1):1-6.
117. Wolcott R G; Boyer P D. The reversal of the myosin and actomyosin ATPase reactions and the free energy of ATP binding to myosin. Biochemical and biophysical research communications 1974;57(3):709-16.
118. Chude O; Boyer P D. Protein-bound sulfhydryl groups and thiolesters in mitochondria and submitochondrial particles and their relationships to oxidative phosphorylation. Archives of biochemistry and biophysics 1974;160(2):366-71.
119. Degani C; Dahms A S; Boyer P D. Characterization of acyl phosphate in transport ATPase by a borohydride reduction method. Annals of the New York Academy of Sciences 1974;242(0):77-9.
120. Dahms A S; Boyer P D. Oxygen exchanges catalyzed by and the mechanism of acyl phosphate formation in transport ATPases. Annals of the New York Academy of Sciences 1974;242(0):133-8.
121. Degani C; Boyer P D. A borohydride reduction method for characterization of the acyl phosphate linkage in proteins and its application to sarcoplasmic reticulum adenosine triphosphatase. The Journal of biological chemistry 1973;248(23):8222-6.
122. Dahms A S; Kanazawa T; Boyer P D. Source of the oxygen in the C-O-P linkage of the acyl phosphate in transport adenosine triphosphatases. The Journal of biological chemistry 1973;248(19):6592-5.
123. Boyer P D.; Cross R L; Momsen W A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions. Proceedings of the National Academy of Sciences of the United States of America 1973;70(10):2837-9.
124. Kanazawa T; Boyer P D. Occurrence and characteristics of a rapid exchange of phosphate oxygens catalyzed by sarcoplasmic reticulum vesicles. The Journal of biological chemistry 1973;248(9):3163-72.
125. Dahms A S; Boyer P D. Occurrence and characteristics of 18 O exchange reactions catalyzed by sodium- and potassium-dependent adenosine triphosphatases. The Journal of biological chemistry 1973;248(9):3155-62.
126. Wolcott R G; Boyer P D. On the nature of p-nitrothiophenylated myosin. Biochimica et biophysica acta 1973;303(2):292-7.
127. Cross R L; Boyer P D. Evidence for detection of AT 32 P bound at the coupling sites of mitochondrial oxidative phosphorylation. Biochemical and biophysical research communications 1973;51(1):59-66.
128. Wedler F C; Boyer P D. Mechanisms of enzyme control as probed by equilibrium exchange rates: patterns of modifier effects with a two substrate, two product system. Journal of theoretical biology 1973;38(3):539-58.
129. Berman K; Boyer P D. Characteristics of the reversible heat, solvent, and detergent denaturation of leucine binding protein. Biochemistry 1972;11(25):4650-7.
130. Klein W L; Boyer P D. Energization of active transport by Escherichia coli. The Journal of biological chemistry 1972;247(22):7257-65.
131. Chaney S G; Duffy J J; Boyer P D. Patterns of oxygen interchange between water, substrates, and phosphate compounds of Escherichia coli and Bacillus subtilis. The Journal of biological chemistry 1972;247(7):2145-50.
132. Chaney S G; Boyer P D. Incorporation of water oxygens into intracellular nucleotides and RNA. II. Predominantly hydrolytic RNA turnover in Escherichia coli. Journal of molecular biology 1972;64(3):581-91.
133. Duffy J J; Chaney S G; Boyer P D. Incorporation of water oxygens into intracellular nucleotides and RNA. I. Predominantly non-hydrolytic RNA turnover in Bacillus subtilis. Journal of molecular biology 1972;64(3):565-79.
134. Wedler F C; Boyer P D. Action patterns of feedback modifiers on equilibrium exchanges and applications to glutamine synthetase (Escherichia coli W). The Journal of biological chemistry 1972;247(4):993-1000.
135. Wedler F C; Boyer P D. Substrate binding and reaction intermediates of glutamine synthetase (Escherichia coli W) as studied by isotope exchanges. The Journal of biological chemistry 1972;247(4):984-92.
136. Leitzmann C; Wu J Y; Boyer P D. Subunits, composition, and related properties of succinyl coenzyme A synthetase. Biochemistry 1970;9(11):2338-46.
137. Hansen J N; Dinovo E C; Boyer P D. Initial and equilibrium 18O, 14C, 3H, and 2H exchange rates as probes of the fumarase reaction mechanism. The Journal of biological chemistry 1969;244(22):6270-9.
138. Chaney S G; Boyer P D. Lack of detection of intermediates in the path of phosphate oxygen to water in photophosphorylation. The Journal of biological chemistry 1969;244(21):5773-6.
139. Jones D H; Boyer P D. The apparent absolute requirement of adenosine diphosphate for the inorganic phosphate–water exchange of oxidative phosphorylation. The Journal of biological chemistry 1969;244(21):5767-72.
140. Kaplan A; Boyer P D. Exchange and localization of 3H and 180 from water and substrates by mitochondria. The Journal of biological chemistry 1969;244(17):4659-63.
141. Robinson J L; Benson R W; Boyer P D. Dephosphorylation of succinyl coenzyme A synthetase as related to enzyme specificity and catalytic intermediates. Biochemistry 1969;8(6):2503-8.
142. Benson R W; Robinson J L; Boyer P D. Quantitative appraisals of possible catalytic intermediates in the succinyl coenzyme A synthetase reaction. Biochemistry 1969;8(6):2496-502.
143. Benson R W; Boyer P D. The participation of an enzyme-bound oxygen group in a coenzyme A transferase reaction. The Journal of biological chemistry 1969;244(9):2366-71.
144. Boyer P D. The inhibition of pyruvate kinase by ATP: a Mg++ buffer system for use in enzyme studies. Biochemical and biophysical research communications 1969;34(5):702-6.
145. Lombardini J B; Singer T P; Boyer P D. Cystein oxygenase. II. Studies on the mechanism of the reaction with 18oxygen. The Journal of biological chemistry 1969;244(5):1172-5.
146. Bridger W A; Millen W A; Boyer P D. Substrate synergism and phosphoenzyme formation in catalysis by succinyl coenzyme A synthetase. Biochemistry 1968;7(10):3608-16.
147. Hill R D; Ford S; Byington K H; Tzagoloff A; Boyer P D. Properties of a polar 32P-phospholipid isolated from a particulate mitochondrial ATPase. Archives of biochemistry and biophysics 1968;127(1):756-65.
148. Kaplan A; Boyer P D. Catalysis of water oxygen and of acetate incorporation into fatty acids by Escherichia coli fatty acid synthetase. The Journal of biological chemistry 1968;243(15):4077-82.
149. Shavit N; Skye G E; Boyer P D. Occurrence and possible mechanism of 32P and 18O exchange reactions of photophosphorylation. The Journal of biological chemistry 1967;242(21):5125-30.
150. Hill R D; Boyer P D. Inorganic orthophosphate activation and adenosine diphosphate as the primary phosphoryl acceptor in oxidative phosphorylation. The Journal of biological chemistry 1967;242(19):4320-3.
151. Moyer R W; Ramaley R F; Butler L G; Boyer P D. The formation and reactions of a nonphosphorylated high energy form of succinyl coenzyme A synthetase. The Journal of biological chemistry 1967;242(19):4299-309.
152. Ramaley R F; Bridger W A; Moyer R W; Boyer P D. The preparation, properties, and reactions of succinyl coenzyme A synthetase and its phosphorylated form. The Journal of biological chemistry 1967;242(19):4287-98.
153. Skye G E; Shavit N; Boyer P D. The catalysis by modified chloroplasts of the Pi-ATP, Pi-HOH and ATP-HOH exchange reactions in the absence of light. Biochemical and biophysical research communications 1967;28(5):724-9.
154. Mitchell R A; Hill R D; Boyer P D. Mechanistic implications of Mg++, adenine nucleotide, and inhibitor effects on energy-linked reactions of submitochondrial particles. The Journal of biological chemistry 1967;242(8):1793-801.
155. Shavit N; Boyer P D. Source of oxygen in adenosine triphosphate formed by illumination or by acid-base transition of chloroplasts. The Journal of biological chemistry 1966;241(23):5738-40.
156. Boyer P D.; Bieber L L; Mitchell R A; Szabolcsi G The apparent independence of the phosphorylation and water formation reactions from the oxidation reactions of oxidative phosphorylation. The Journal of biological chemistry 1966;241(22):5384-90.
157. Bieber L L; Boyer P D. 32P-labeling of mitochondrial protein and lipid fractions and their relation to oxidative phosphorylation. The Journal of biological chemistry 1966;241(22):5375-83.
158. Sartorelli L; Fromm H J; Benson R W; Boyer P D. Direct and 18-O-exchange measurements relevant to possible activated or phosphorylated states of myosin. Biochemistry 1966;5(9):2877-84.
159. Richards O C; Boyer P D. 18O labeling of deoxyribonucleic acid during synthesis and stability of the label during replication. Journal of molecular biology 1966;19(1):109-19.
160. Hultquist D E; Moyer R W; Boyer P D. The preparation and characterization of 1-phosphohistidine and 3-phosphohistidine. Biochemistry 1966;5(1):322-31.
161. Boyer P D.; Slater E C Labelling rates and detection of intermediates in mitochondrial phosphorylations and other sequential reactions. Nature 1965;207(995):409-12.
162. Norman A W; Bieber L L; Lindberg O; Boyer P D. Relationships Of Ca++ To ”Protein-Bound” Phosphate Fractions Of Mitochondria. The Journal of biological chemistry 1965;240():2855-62.
163. Lindberg o; duffy j j; norman a w; boyer P D. characteristics of bound phosphohistidine labeling in mitochondria. The Journal of biological chemistry 1965;240():2850-4.
164. HINKSON J W; BOYER P D. The Light-Induced Formation Of Rapidly Phosphorylated Compounds In Chloroplasts. Archives of biochemistry and biophysics 1965;110():16-22.
165. Richards o c; boyer P D. chemical mechanism of sonic, acid, alkaline and enzymic degradation of dna. Journal of molecular biology 1965;11():327-40.
166. Silverstein e; boyer P D. equilibrium reaction rates and the mechanisms of liver and yeast alcohol dehydrogenase. The Journal of biological chemistry 1964;239():3908-14.
167. Silverstein e; boyer P D. equilibrium reaction rates and the mechanisms of bovine heart and rabbit muscle lactate dehydrogenases. The Journal of biological chemistry 1964;239():3901-7.
168. Fromm h j; silverstein e; boyer P D. equilibrium and net reaction rates in relation to the mechanism of yeast hexokinase. The Journal of biological chemistry 1964;239():3645-52.
169. Mitchell R A; Butler L G; Boyer P D. The association of readily-soluble bound phosphohistidine from mitochondria with succinate thiokinase. Biochemical and biophysical research communications 1964;16(6):545-50.
170. Kreil G; Boyer P D. Detection of bound phosphohistidine in E. coli succinate thiokinase. Biochemical and biophysical research communications 1964;16(6):551-5.
171. Bieber l l; lindberg o; duffy j j; boyer P D. rate and extent of labelling of bound phosphohistidine as related to its role in mitochondria. Nature 1964;202():1316-8.
172. Boyer P D. Phosphohistidine. Science (New York, N.Y.) 1963;141():1147-53.
173. Boyer P D. phosphohistidine. Science (New York, N.Y.) 1963;141():1147-53.
174. Westhead e w; butler l; boyer P D. binding sites, reactivation phenomena, and possible -s-s- groups of rabbit muscle aldolase. Biochemistry 1963;2():927-34.
175. Dempsey M E; Boyer P D.; Benson E S Characteristics Of An Orthophosphate Oxygen Exchange Catalyzed By Myosin, Actomyosin, And Muscle Fibers. The Journal of biological chemistry 1963;238():2708-15.
176. Boyer P D.; Hultquist D E; Peter J B; Kreil G; Mitchell R A; Deluca M; Hinkson J W; Butler L G; Moyer R W Role Of The Phosphorylated Imidazole Group In Phosphorylation And Energy Transfer Reactions. Federation proceedings 1963;22():1080-7.
177. Peter J B; Hultquist D E; Deluca M; Kreil G; Boyer P D. Bound phosphohistidine as an intermediate in a phosphorylation reaction of oxidative phosphorylation catalyzed by mitochondrial extracts. The Journal of biological chemistry 1963;238():1182-4.
178. Peter J B; Boyer P D. The formation of bound phosphohistidine from adenosine triphosphate-P32 in mitochondria. The Journal of biological chemistry 1963;238():1180-2.
179. Deluca M; Ebner K E; Hultquist D E; Kreil G; Peter J B; Moyer R W; Boyer P D. The Isolation And Identification Of Phosphohistidine From Mitochondrial Protein. Biochemische Zeitschrift 1963;338():512-25.
180. Jenne J W; Boyer P D. Kinetic characteristics of the acetylation of isoniazid and p-aminosalicylic acid by a liver-enzyme preparation. Biochimica et biophysica acta 1962;65():121-7.
181. Jenne J W; Boyer P D. Kinetic characteristics of the acetylation of isoniazid and p-aminosalicylic acid by a liver-enzyme preparation. Biochimica et biophysica acta 1962;65():121-7.
182. Boyer P D.; Deluca M; Ebner K E; Hultquist D E; Peter J B Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation. The Journal of biological chemistry 1962;237():PC3306-PC3308.
183. Graves D J; Boyer P D. Substrate interchanges and oxygen transfers catalyzed by glutamine synthetase at equilibrium. Biochemistry 1962;1():739-47.
184. Kaziro Y; Hass L F; Boyer P D.; Ochoa S Mechanism of the propionyl carboxylase reaction. II. Isotopic exchange and tracer experiments. The Journal of biological chemistry 1962;237():1460-8.
185. Graves D J; Boldt R E; Boyer P D. The lack of incorporation of canavanine into rabbit-muscle protein in vivo. Biochimica et biophysica acta 1962;57():165-7.
186. Westhead E W; Boyer P D. The incorporation of p-fluorophenylalanine into some rabbit enzymes and other proteins. Biochimica et biophysica acta 1961;54():145-56.
187. Suelter C H; Deluca M; Peter J B; Boyer P D. Detection of a possible intermediate in oxidative phosphorylation. Nature 1961;192():43-7.
188. Reynard A M; Hass L F; Jacobsen D D; Boyer P D. The correlation of reaction kinetics and substrate binding with the mechanism of pyruvate kinase. The Journal of biological chemistry 1961;236():2277-83.
189. Hass L F; Boyer P D.; Reynard A M Studies on possible phosphoryl enzyme formation in catalysis by hexokinase, pyruvate kinase, and glucose 6-phosphatase. The Journal of biological chemistry 1961;236():2284-91.
190. Schulz A R; Boyer P D. The fate of oxygens of inorganic phosphate in photophosphorylation. Archives of biochemistry and biophysics 1961;93():335-7.
191. Dempsey M E; Boyer P D. Catalysis of an inorganic phosphate-H2-O-18 exchange by actomysin and myosin. The Journal of biological chemistry 1961;236():PC6-PC7.
192. Kowalsky A; Boyer P D. A carboxypeptidase-O18-labeled water procedure for determination of CO OH-terminal residues and its application to aldolase. The Journal of biological chemistry 1960;235():604-8.
193. Boyer P D. Mechanism of enzyme action. Annual review of biochemistry 1960;29():15-44.
194. Drechsler E R; Boyer P D.; Kowalsky A G The catalytic activity of carboxypeptidase-degraded aldolase. The Journal of biological chemistry 1959;234():2627-34.
195. FALCONE A B; BOYER P D. Studies concerning the mechanism of action of acetoacetyl succinic thiophorase by use of O18. Archives of biochemistry and biophysics 1959;83(1):337-44.
196. Boyer P D.; Bier M F. F. Nord: dedication. Archives of biochemistry and biophysics 1959;83(1):1.
197. Boyer P D. Uses and limitations of measurements of rates of isotopic exchange and incorporation in catalyzed reactions. Archives of biochemistry and biophysics 1959;82(2):387-410.
198. Boyer P D.; Mills R C; Fromm H J Hypotheses for and some kinetic studies with glutamine synthetase and acetate thiokinase. Archives of biochemistry and biophysics 1959;81(1):249-63.
199. Boyer P D.; Stulberg M P Tracing of the In Vivo Path from Amino Acid to Protein. Proceedings of the National Academy of Sciences of the United States of America 1958;44(2):92-7.
200. Hoagland M B; Zamecnik P C; Sharon N; Lipmann F; Stulberg M P; Boyer P D. Oxygen transfer to AMP in the enzymic synthesis of the hydroxamate of tryptophan. Biochimica et biophysica acta 1957;26(1):215-7.
201. Gander J E; Petersen W E; BOYER P D. On the enzymic synthesis of lactose-1-PO4. Archives of biochemistry and biophysics 1957;69():85-99.
202. Boyer P D.; Robbins E A Determination of the equilibrium of the hexokinase reaction and the free energy of hydrolysis of adenosine triphosphate. The Journal of biological chemistry 1957;224(1):121-35.
203. Boyer P D.; Falcone A B; Luchsinger W W O18 and P32 exchange reactions of mitochondria in relation to oxidative phosphorylation. The Journal of biological chemistry 1956;223(1):405-21.
204. Blakley E R; Boyer P D.; Gander J E; Harrison W H Interconversions of alpha-tocopherol and its oxidation products. Biochimica et biophysica acta 1956;21(1):150-8.
205. Robertson H E; Boyer P D. Orthophosphite as a buffer for biological studies. Archives of biochemistry and biophysics 1956;62(2):396-401.
206. Robertson H E; Boyer P D. The biological inactivity of glucose 6-phosphite, inorganic phosphites and other phosphites. Archives of biochemistry and biophysics 1956;62(2):380-95.
207. Koeppe O J; Boyer P D.; Stulberg M P On the occurrence, equilibria, and site of acyl-enzyme formation of glyceraldehyde-3-phosphate dehydrogenase. The Journal of biological chemistry 1956;219(2):569-83.
208. Gander J E; Petersen W E; Boyer P D. On the mechanism of the enzymatic synthesis of lactose. Archives of biochemistry and biophysics 1956;60(1):259-61.
209. Harrison W H; Boyer P D.; Falcone A B The mechanism of enzymic phosphate transfer reactions. The Journal of biological chemistry 1955;215(1):303-17.
210. Robertson H E; Boyer P D. The effect of azide on phosphorylation accompanying electron transport and glycolysis. The Journal of biological chemistry 1955;214(1):295-305.
211. Blakley E R; Boyer P D. The effect of 6-deoxy-6-fluoro-d-glucose on yeast fermentation and on hexokinase. Biochimica et biophysica acta 1955;16(4):576-82.
212. Robbins E A; Stulberg M P; Boyer P D. The magnesium activation of pyrophosphatase. Archives of biochemistry and biophysics 1955;54(1):215-22.
213. Boyer P D. Fat-soluble vitamins. Annual review of biochemistry 1955;24():465-96.
214. Boyer P D.; Falcone A B; Harrison W H Reversal and mechanism of oxidative phosphorylation. Nature 1954;174(4426):401-2.
215. Segal H L; Boyer P D. The role of sulfhydryl groups in the activity of D-glyceraldehyde 3-phosphate dehydrogenase. The Journal of biological chemistry 1953;204(1):265-81.
216. Boyer P D. The activation by K+ and occurrence of pyruvic phosphoferase in different species. Journal of cellular physiology 1953;42(1):71-7.
217. Boyer P D. The role of potassium and related cations in the action of pyruvic phosphoferase and other enzymes. The Journal-lancet 1953;73(5):195-6.
218. Kachmar J F; Boyer P D. Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase. The Journal of biological chemistry 1953;200(2):669-82.
219. Tappel A L; Lundberg W O; Boyer P D. Effect of temperature and antioxidants upon the lipoxidase-catalyzed oxidation of sodium linoleate. Archives of biochemistry and biophysics 1953;42(2):293-304.
220. Tappel A L; Boyer P D.; Lundberg W O The reaction mechanism of soy bean lipoxidase. The Journal of biological chemistry 1952;199(1):267-81.
221. Turner E W; Boyer P D. Interaction of protein antigens and antibodies. III. Dissociation studies with diphtheria toxoid-antitoxin precipitates. Journal of immunology (Baltimore, Md. : 1950) 1952;69(3):265-71.
222. Kleinschmidt W J; Boyer P D. Interaction of protein antigens and antibodies. I. Inhibition studies with the egg albumin-antiegg albumin system. Journal of immunology (Baltimore, Md. : 1950) 1952;69(3):247-55.
223. Turner E W; Boyer P D. Combinations of modified serum gamma-globulin with other proteins. Archives of biochemistry and biophysics 1952;37(2):353-65.
224. Segal H L; Kachmar J F; Boyer P D. Kinetic analysis of enzyme reactions. I. Further considerations of enzyme inhibition and analysis of enzyme activation. Enzymologia 1952;15(4):187-98.
225. Rabinovitz M; Stulberg M P; Boyer P D. The control of pyruvate oxidation in a cell-free rat heart preparation by phosphate acceptors. Science (New York, N.Y.) 1951;114(2972):641-2.
226. : Boyer P D.; Rabinovitz M; Liebe E Chemical structure in relation to vitamin E function. The Journal of biological chemistry 1951;192(1):95-103.
227. Rabinovitz M; Boyer P D. Oxidative phosphorylation of heart tissue from vitamin E deficient rabbits. Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.) 1951;77(1):103-5.
228. Kachmar J F; Boyer P D.; Gullickson T W; Liebe E; Porter R M Vitamin E in the nutrition of cattle. II. Vitamin E levels in the blood, vitamin A and carotene utilization, and other chemical studies. The Journal of nutrition 1950;42(3):391-403.
229. Wolcott G H; Boyer P D. A colorimetric method for the determination of citric acid in blood and plasma. The Journal of biological chemistry 1948;172(2):729-36.
230. Ballou G A; Boyer P D.; Luck J M; Lum F G 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. The Journal of clinical investigation 1944;23(4):454-7.
Photos of Paul D. Boyer
