Thermodynamic volume cycles for electron transfer in the cytochrome c oxidase and for the binding of cytochrome c to cytochrome c oxidase

Biophysical Journal

Volumn 75, Issue 1, 1998, Pages 435-444

  Kornblatt, Jack A ^a   Kornblatt, Mary Judith ^a   Rajotte, Isabelle ^a   Hoa, Gaston Hui Bon ^b   Kahn, Peter C ^c  

^a Gina Cody School of Engineering and Computer Science   (Canada)

^b INST DE BIOLOGIE PHYSICO CHIMIQUE   (France)

^c RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; CYTOCHROME C OXIDASE;

ARTICLE; CHEMICAL REACTION KINETICS; ELECTRON TRANSPORT; ENZYME ANALYSIS; ENZYME BINDING; ENZYME PURIFICATION; HUMAN; HUMAN CELL; HUMAN TISSUE; HYDRATION; OXIDATION REDUCTION REACTION; PROTEIN STRUCTURE; STOICHIOMETRY; THERMODYNAMICS;

EID: 0031836877     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77531-9     Document Type: Article

References (53)

1. Babcock, G. T., and M. Wikström. 1992. Oxygen activation and the conservation of energy in cell respiration. Nature. 356:301-309.
2. B. Biochemistry. 34:7967-7972.
3. Bhat, T. N., G. A. Bentley, G. Boulot, M. I. Greene, D. Tello, W. Dall'Acqua, H. Souchon, F. P. Schwartz, R. A. Mariuzza, and R. J. Poljak. 1994. Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Proc. Natl. Acad. Sci. USA. 91:1089-1093.
4. Bisson, R., B. Jacobs, and R. A. Capaldi. 1980. Binding of arylazidocytochrome c derivatives to beef heart cytochrome c oxidase. Biochemistry. 19:4173-4178.
5. Cao, Y., G. Váró, M. Chang, R. Needleman, and J. Lanyi. 1991. Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff base. Biochemistry. 30:10972-10979.
6. Cruañes, M. T., K. K. Rodgers, and S. G. Sligar. 1992. Protein chemistry at high pressure. J. Am. Chem. Soc. 114:9660-9661.
7. Deatherage, J. F., and R. Henderson. 1982. Three-dimensional structure of cytochrome c oxidase vesicle crystals in negative stain. J. Mol. Biol. 158:487-499.
8. Ermler, U., G. Fritzsch, S. K. Buchanan, and H. Michel. 1994. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure. 2:925-936.
9. Ferguson-Miller, S., D. L. Brautigan, and E. Margoliash. 1978. Definition of cytochrome c binding domains by chemical modification. J. Biol. Chem. 253:149-159.
10. Foygel, K., S. Spector, S. Chattergee, and P. C. Kahn. 1995. Volume changes of the molten globule transitions of horse heart ferricytochrome c: a thermodynamic cycle. Protein Sci. 4:1426-1429.
11. Gennis, R., and S. Ferguson-Miller. 1995. Structure of cytochrome c oxidase, energy generator of aerobic life. Science. 269:1063-1064.
12. Greenwood, C., M. T. Wilson, and M. Brunori. 1974. Studies on partially reduced mammalian cytochrome oxidase. Biochem. J. 137:205-215.
13. Gross, M., and R. Jaenicke. 1994. Proteins under pressure. Eur. J. Biochem. 221:617-630.
14. Hill, B. C. 1994a. Modeling the sequence of electron transfer reactions in the single turnover of reduced cytochrome c oxidase with oxygen. J. Biol. Chem. 269:2419-2425.
15. Hill, B. C. 1994b. The pathway of CO binding to cytochrome c oxidase: can the gateway be closed? FEBS Lett. 354:284-288.
16. Hummel, J. P., and W. J. Dreyer. 1962. Measurement of protein-binding phenomena by gel filtration. Biochim. Biophys. Acta. 63:530-532.
17. Iwata, S., C. Ostermeier, B. Ludwig, and H. Michel. 1995. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:660-669.
18. Johnson, M. K., D. G. Englinton, P. E. Gooding, C. Greenwood, and A. J. Thomson. 1981. Characterization of the partially reduced cyanide-inhibited derivative of cytochrome c oxidase by optical, electron-paramagnetic-resonance and magnetic-circular dichroism spectroscopy. Biochem. J. 193:699-708.
19. Kahn, P. C., and R. W. Briehl. 1982. The absence of volume change in the gelation of hemoglobin-s. J. Biol. Chem. 257:12209-12213.
20. Kauzmann, W. 1959. Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 14:1-63
21. Kornblatt, J. A., and G. Hui Bon Hoa. 1990. A non-traditional role for water in the cytochrome c oxidase reaction. Biochemistry. 29: 9370-9376.
22. Kornblatt, J. A., G. Hui Bon Hoa, and A. M. English. 1984. Volume changes associated with the cytochrome c oxidase/porphyrin c equilibrium. Biochemistry. 23:5906-5911.
23. Kornblatt, J. A., G. Hui Bon Hoa, and K. Heremans. 1988. Effects of pressure on cytochrome oxidase: the aerobic steady state. Biochemistry. 27:5122-5128.
24. Kornblatt, J. A., and M. J. Kornblatt. 1992. Cytochrome c oxidase: the presumptive channel holds at least four water molecules. Biochim. Biophys. Acta. 1099:182-184.
25. Kornblatt, J. A., M. J. Kornblatt, and G. Hui Bon Hoa. 1995. Second derivative spectroscopy of enolase at high pressure. Biochemistry. 34: 1218-1223.
26. Kornblatt, J. A., M. J. Kornblatt, G. Hui Bon Hoa, and A. G. Mauk. 1993. Responses of two protein-protein complexes to solvent stress: does water play a role at the interface? Biophys. J. 65:1059-1065.
27. Kornblatt, J. A., and H. A. Luu. 1986. Porphyrin cytochrome c-cytochrome c oxidase interactions: the resting, reduced and pulsed enzymes. Eur. J. Biochem. 159:407-413.
28. Kroneck, P. M. H., W. A. Antholine, J. Riester, and W. G. Zumft. 1988. The cupric site in nitrous oxide reductase contains a mixed-valence [Cu(II), Cu(I)] binuclear center: a multifrequency electron paramagnetic resonance investigation. FEBS Lett. 242:70-74.
29. Linderstrom-Lang, K., and H. Lanz. 1938. C. R. Trav. Lab. Carlsberg Ser. Chim. 21:315-338.
30. Malmstrom, B. G. 1993. Vectorial chemistry in bioenergetics: cytochrome c oxidase as a redox-linked proton pump. Acc. Chem. Res. 26:332-338.
31. Margoliash, E., and H. R. Bosshard. 1983. A textbook protein comes of age. Trends Biochem. Sci. 8:316-320.
32. Martinez, S. E., D. Huang, M. Ponomarev, W. A. Cramer, and J. L. Smith. 1996. The heme linked redox center of chloroplast cytochrome f is linked to a buried five water chain. Protein Sci. 5:1081-1092.
33. Mochan, E., and P. Nicholls. 1972. Cytochrome c reactivity in its complexes with mammalian cytochrome c oxidase and yeast peroxidase. Biochim. Biophys. Acta. 267:309-319.
34. Nicholls, P. 1979a. In Oxidases and Related Redox Systems III, Proceedings of the Third ISOX Symposium, Albany, NY. T. E. King, H. S. Mason, and M. Morrison, editors. Pergamon Press, Tarrytown, NY.
35. Nicholls, P. 1979b. Effects of inhibitory ligands on the aerobic carbon monoxide complex of cytochrome c oxidase. Biochem. J. 183:519-529.
36. Nicholls, P. N., Y. Sternin, J. Loewen, and B. Tattrie. 1996. Hydration as a control mechanism in membrane proteins: the case of cytochrome c oxidase. Faraday Discuss. 103:313-323.
37. Ogunmola, G. B., W. Kauzmann, and A. Zipp. 1976. Volume changes on binding of ligands to methemoglobin and metmyoglobin. Proc. Natl. Acad. Sci. USA. 73:4271-4273.
38. Paladini, A. A., and G. Weber. 1981. Reversible dissociation of enolase. Biochemistry. 20:2587-2593.
39. Parsegian, V. A., R. P. Rand, and D. C. Rau. 1995. Macromolecules and water: probing with osmotic stress. Methods Enzymol. 259:43-94.
40. Pelletier, H., and J. Kraut. 1992. Crystal structure of a complex between electron transfer partners cytochrome c peroxidase and cytochrome c. Science. 258:1748-1755.
41. Privalov, P. L. 1979. Energetics of protein structure. Adv. Protein Sci. 33:167-241.
42. 5-cytochrome c complex. Science. 240:1657-1659.
43. Salmon, E. D. 1975. Pressure induced depolymerization of brain microtubules in vitro. Science. 189:884-886.
44. Tsukihara, T., H. Aoyama, E. Yamashita, T. Tomazaki, H. Yamaguchi, K. Shinzawa-Itoh, R. Nakashima, R. Yano, and S. Yoshikawa. 1995. Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å. Science. 269:1069-1074.
45. Tsukihara, T., H. Aoyama, E. Yamashita, T. Tomazaki, H. Yamaguchi, K. Shinzawa-Itoh, R. Nakashima, R. Yano, and S. Yoshikawa. 1996. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science. 272:1136-1144.
46. Varo, G., and J. K. Lanyi. 1995. Effects of hydrostatic pressure on the kinetics reveal a volume increase during the bacteriorhodopsin photocycle. Biochemistry. 34:12161-12169.
47. Varo, G., R. Needleman, and J. K. Lanyi. 1995. Light driven chloride uptake by halorhodopsin from Natrium pharonis. Biochemistry. 34: 14500-14507.
48. Wikstrom, M., K. Krab, and M. Saraste. 1981. Cytochrome c Oxidase: A Synthesis. Academic Press, New York.
49. Williams, R. J. P. 1995. Purpose of proton pathways. Nature. 376:643.
50. Wilmanns, M., P. Lappalainen, M. Kelly, E. Sauer-Ericksson, and M. Saraste. 1995. Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center. Proc. Natl. Acad. Sci. USA. 92:11955-11959.
51. Yamazaki, Y., M. Hatanaka, H. Kandori, J. Sasaki, W. F. J. Karstens, J. Raap, J. Lutgenburg, M. Bisounok, J. Herzfeld, R. Needleman, J. Lanyi, and A. Maeda. 1995. Water structural changes at the proton uptake site in the L intermediate of bacteriorhodopsin. Biochemistry. 34: 7088-7093.
52. Yonetani, T. 1966. Cytochrome oxidase from beef heart. Biochem. Prep. 11:14-20.
53. Zhang, W., M. W. Capp, J. P. Bond, C. F. Anderson, and M. T. Record. 1996. Thermodynamic characterization of native BSA with highly excluded (glycine betaine) and moderately accumulated (urea) solutes by a novel application of vapor pressure osmometry. Biochemistry. 35: 10506-10516.