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. 1968 Sep;61(1):277–283. doi: 10.1073/pnas.61.1.277

The role of Factor B in the energy transfer reactions of oxidative phosphorylation.

D R Sanadi, K W Lam, C K Kurup
PMCID: PMC285933  PMID: 4301590

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ANDREOLI T. E., LAM K. W., SANADI D. R. STUDIES ON OXIDATIVE PHOSPHORYLATION. X. A COUPLING ENZYME WHICH ACTIVATES REVERSED ELECTRON TRANSFER. J Biol Chem. 1965 Jun;240:2644–2653. [PubMed] [Google Scholar]
  2. 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. J Biol Chem. 1966 Nov 25;241(22):5384–5390. [PubMed] [Google Scholar]
  3. COOPER C., LEHNINGER A. L. Oxidative phosphorylation by an enzyme complex from extracts of mitochondria. III. The span cytochrome c to oxygen. J Biol Chem. 1956 Mar;219(1):519–529. [PubMed] [Google Scholar]
  4. Chance B., Mela L. Hydrogen ion concentration changes in mitochondrial membranes. J Biol Chem. 1966 Oct 25;241(20):4588–4599. [PubMed] [Google Scholar]
  5. FLUHARTY A. L., SANADI D. R. ON THE MECHANISM OF OXIDATIVE PHOSPHORYLATION. VI. LOCALIZATION OF THE DITHIOL IN OXIDATIVE PHOSPHORYLATION WITH RESPECT TO THE OLIGOMYCIN INHIBITION SITE. Biochemistry. 1963 May-Jun;2:519–522. doi: 10.1021/bi00903a022. [DOI] [PubMed] [Google Scholar]
  6. Fessenden J. M., Dannenberg M. A., Racker E. Effect of coupling factor 3 on oxidative phosphorylation. Biochem Biophys Res Commun. 1966 Oct 5;25(1):54–59. doi: 10.1016/0006-291x(66)90639-5. [DOI] [PubMed] [Google Scholar]
  7. Fluharty A., Sanadi D. R. EVIDENCE FOR A VICINAL DITHIOL IN OXIDATIVE PHOSPHORYLATION. Proc Natl Acad Sci U S A. 1960 May;46(5):608–616. doi: 10.1073/pnas.46.5.608. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fonyo A., Bessman S. P. The action of oligomycin and of para-hydroxymercuribenzoate on mitochondrial respiration stimulated by ADP, arsenate and calcium. Biochem Biophys Res Commun. 1966 Jul 6;24(1):61–66. doi: 10.1016/0006-291x(66)90410-4. [DOI] [PubMed] [Google Scholar]
  9. HOMMES F. A. Kinetics of succinate linked pyridine nucleotide reduction in sonic particles from beef heart mitochondria. Biochem Biophys Res Commun. 1962 Jul 19;8:248–252. doi: 10.1016/0006-291x(62)90272-3. [DOI] [PubMed] [Google Scholar]
  10. LINNANE A. W. A soluble component required for oxidative phosphorylation by a sub-mitochondrial particle from beef heart muscle. Biochim Biophys Acta. 1958 Oct;30(1):221–222. doi: 10.1016/0006-3002(58)90281-6. [DOI] [PubMed] [Google Scholar]
  11. LINNANE A. W., ZIEGLER D. M. Studies on the mechanism of oxidative phosphorylation. V. The phosphorylating properties of the electron transport particle. Biochim Biophys Acta. 1958 Sep;29(3):630–638. doi: 10.1016/0006-3002(58)90021-0. [DOI] [PubMed] [Google Scholar]
  12. Lam K. W. Sulfhydryl group involvement in a soluble energy transfer factor of the oxidative phosphorylation system. Arch Biochem Biophys. 1968 Mar 11;123(3):642–643. doi: 10.1016/0003-9861(68)90186-0. [DOI] [PubMed] [Google Scholar]
  13. Lam K. W., Warshaw J. B., Sanadi D. R. The mechanism of oxidative phosphorylation. XIV. Purification and properties of a second energy-transfer factor. Arch Biochem Biophys. 1967 Mar;119(1):477–484. doi: 10.1016/0003-9861(67)90479-1. [DOI] [PubMed] [Google Scholar]
  14. MacLennan D. H., Tzagoloff A. Studies on the mitochondrial adenosine triphosphatase system. IV. Purification and characterization of the oligomycin sensitivity conferring protein. Biochemistry. 1968 Apr;7(4):1603–1610. doi: 10.1021/bi00844a050. [DOI] [PubMed] [Google Scholar]
  15. PENEFSKY H. S., PULLMAN M. E., DATTA A., RACKER E. Partial resolution of the enzymes catalyzing oxidative phosphorylation. II. Participation of a soluble adenosine tolphosphatase in oxidative phosphorylation. J Biol Chem. 1960 Nov;235:3330–3336. [PubMed] [Google Scholar]
  16. PENEFSKY H. S., PULLMAN M. E., DATTA A., RACKER E. Partial resolution of the enzymes catalyzing oxidative phosphorylation. II. Participation of a soluble adenosine tolphosphatase in oxidative phosphorylation. J Biol Chem. 1960 Nov;235:3330–3336. [PubMed] [Google Scholar]
  17. PRAIRIE R. L., CONOVER T. E., RACKER E. Requirement for multiple factors for the ATP-linked reduction of DPN by succinate. Biochem Biophys Res Commun. 1963 Mar 5;10:422–427. doi: 10.1016/0006-291x(63)90549-7. [DOI] [PubMed] [Google Scholar]
  18. PULLMAN M. E., PENEFSKY H., RACKER E. A soluble protein fraction required for coupling phosphorylation to oxidation in submitochondrial fragments of beef heart mitochondria. Arch Biochem Biophys. 1958 Jul;76(1):227–230. doi: 10.1016/0003-9861(58)90138-3. [DOI] [PubMed] [Google Scholar]
  19. PULLMAN M. E., PENEFSKY H., RACKER E. A soluble protein fraction required for coupling phosphorylation to oxidation in submitochondrial fragments of beef heart mitochondria. Arch Biochem Biophys. 1958 Jul;76(1):227–230. doi: 10.1016/0003-9861(58)90138-3. [DOI] [PubMed] [Google Scholar]
  20. Penniston J. T., Harris R. A., Asai J., Green D. E. The conformational basis of energy transformations in membrane systems. I. Conformational changes in mitochondria. Proc Natl Acad Sci U S A. 1968 Feb;59(2):624–631. doi: 10.1073/pnas.59.2.624. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. RACKER E. A mitochondrial factor conferring oligomycin sensitivity on soluble mitochondrial ATPase. Biochem Biophys Res Commun. 1963 Mar 25;10:435–439. doi: 10.1016/0006-291x(63)90375-9. [DOI] [PubMed] [Google Scholar]
  22. RACKER E., CONOVER T. E. MULTIPLE COUPLING FACTORS IN OXIDATIVE PHOSPHORYLATION. Fed Proc. 1963 Jul-Aug;22:1088–1091. [PubMed] [Google Scholar]
  23. RACKER E. Studies of factors involved in oxidative phosphorylation. Proc Natl Acad Sci U S A. 1962 Sep 15;48:1659–1663. doi: 10.1073/pnas.48.9.1659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Racker E., Horstman L. L. Partial resolution of the enzymes catalyzing oxidative phosphorylation. 13. Structure and function of submitochondrial particles completely resolved with respect to coupling factor. J Biol Chem. 1967 May 25;242(10):2547–2551. [PubMed] [Google Scholar]
  25. SANADI D. R., FLUHARTY A. L., ANDREOLI T. E. Partial resolution and reconstitution of the adenosine triphosphate-dependent reduction of diphosphopyridine nucleotide by succinate. Biochem Biophys Res Commun. 1962 Jul 3;8:200–203. doi: 10.1016/0006-291x(62)90263-2. [DOI] [PubMed] [Google Scholar]
  26. Slater E. C. Effect of sulphydryl-combining compounds on the activity of the succinic oxidase system. Biochem J. 1949;45(2):130–142. doi: 10.1042/bj0450130. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Sone N., Hagihara B. A coupling factor of oxidative phosphorylation without adenosine triphosphatase activity from beef heart mitochondria. J Biochem. 1966 Dec;60(6):622–631. doi: 10.1093/oxfordjournals.jbchem.a128488. [DOI] [PubMed] [Google Scholar]
  28. TRUDINGER P. A. Cytochromes and thiosulphate oxidation in an aerobic Thiobacillus. Biochim Biophys Acta. 1958 Oct;30(1):211–212. doi: 10.1016/0006-3002(58)90274-9. [DOI] [PubMed] [Google Scholar]
  29. Vallejos R. H., Slater E. C. A soluble ATPase with high coupling activity. Biochim Biophys Acta. 1967 Sep 6;143(2):441–444. doi: 10.1016/0005-2728(67)90102-8. [DOI] [PubMed] [Google Scholar]
  30. WADKINS C. L., LEHNINGER A. L. The adenosine triphosphate-adenosine diphosphate exchange reaction of oxidative phosphorylation. J Biol Chem. 1958 Dec;233(6):1589–1597. [PubMed] [Google Scholar]
  31. Warshaw J. B., Lam K. W., Nagy B., Sanadi D. R. Studies on oxidative phosphorylation. XV. Latent adenosine 5'-triphosphatase activity of factor A. Arch Biochem Biophys. 1968 Feb;123(2):385–396. doi: 10.1016/0003-9861(68)90149-5. [DOI] [PubMed] [Google Scholar]

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