Energy transduction function of the quinone reactions in cytochrome bc complexes

BioFactors

Volumn 9, Issue 2-4, 1999, Pages 81-86

  Cramer, William A ^a   Soriano, Glenda M ^a  

^a PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

1,4 BENZOQUINONE; CYTOCHROME B; HISTIDINE; HYDROGEN; IRON SULFUR PROTEIN; UBIQUINOL CYTOCHROME C REDUCTASE;

BILAYER MEMBRANE; BINDING SITE; ELECTRON TRANSPORT; ENERGY TRANSFER; MITOCHONDRION; OSMOSIS; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTON TRANSPORT; REVIEW;

MAMMALIA;

EID: 0033000258     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520090201     Document Type: Review

References (22)

1. U. Brandt and J.G. Okun, Role of deprotonation events in ubihydroquinone:cytochrome c oxydoreductase from bovine heart and yeast mitochondria, Biochemistry 36 (1997), 11 234-11 240.
2. C.J. Carrell, H. Zhang, W.A. Cramer and J.L. Smith, Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein, Structure 5 (1998), 1613-1625.
3. F.L. Crane, Y. Hatefi, R.L. Lester and C. Widmer, Isolation of a quinone from beef heart mitochondria, Biochimica et Biophysica Acta 25 (1957), 220-221.
4. 1 complex, Science 281 (1998), 64-71.
5. 1 complex determined by MAD phasing at 1.5 Å resolution, Structure 4 (1996), 567-579.
6. H. Kim, D. Xia, C.A. Yu, J.Z. Xia, A.M. Kachurin, L. Zhang, L. Yu and J. Deisenhofer, Inhibitor binding changes domain mobility in the iron-sulfur protein of the mitochondrial bc1 complex from bovine heart, Proceedings of the National Academy of Sciences, USA 95 (1998), 8026-8033.
7. P.J. Kraulis, MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures, Journal of Applied Crystallography 24 (1991), 946-950.
8. R.L. Lester, F.L. Crane and Y. Hatefi, Coenzyme Q: a new group of quinones, Journal of the American Chemical Society 80 (1958), 4751-4752.
9. T.A. Link, The role of the 'Rieske' iron sulfur protein in the hydroquinone oxidation (Q(P)) site of the cytochrome bc1 complex. The 'proton-gated affinity change' mechanism, FEBS Letters 412 (1997), 257-264.
10. H. Luecke, H.T. Richter and J.K. Lanyi, Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution, Science 280 (1998), 1934-1937.
11. S. Martinez, D. Huang, M. Ponomarev, W.A. Cramer and J.L. Smith, The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain, Protein Science 5 (1996), 1081-1092.
12. P. Mitchell, Chemiosmotic coupling in oxidative and photosynthetic phosphorylation, Biological Reviews of the Cambridge Philosophical Society 41 (1966), 445-502.
13. P. Mitchell, Possible molecular mechanisms of the protonmotive function of cytochrome systems, Journal of Theoretical Biology 62 (1976), 327-367.
14. 6, Biochemistry 37 (1998), 17 199-17 208.
15. P. Rich, Electron and proton transfers through quinones and cytochrome bc complexes, Biochimica et Biophysica Acta 768 (1984), 53-79.
16. P. Rich and D. Bendall, The kinetics and thermodinamics of the reduction of cytochrome c by substituted p-benzoquinols in solution, Biochimica et Biophysica Acta 592 (1980), 506-518.
17. E.L. Ulrich, M.E. Girvin, W.A. Cramer and J.L. Markley, Location and mobility of ubiquinones of different chain lengths in artificial membrane vesicles, Biochemistry 24 (1985), 2501-2508.
18. 6f complex: position of the cytochrome b hemes in the membrane, Proceedings of the National Academy of Sciences, USA 81 (1984), 674-678.
19. M.K.F. Wikström and M. Saraste, The mitochondrial respiratory chain, in: Bioenergetics, L. Ernster, ed., Elsevier, Amsterdam, 1984, pp. 49-94.
20. 1 complex from bovine heart mitochondria, Science 277 (1997), 60-66.
21. H. Zhang, C.J. Carrell, D. Huang, V. Sled, T. Ohnishi, J.L. Smith and W.A. Cramer, Characterization and crystallization of the lumen-side domain of the chloroplast Rieske iron-sulfur protein, Journal of Biological Chemistry 271 (1996), 31 360-31 366.
22. 1, Nature 392 (1998), 677-684.