Plasmon waveguide resonance spectroscopic evidence for differential binding of oxidized and reduced Rhodobacter capsulatus cytochrome c2 to the cytochrome bc1 complex mediated by the conformation of the rieske iron-sulfur protein

Biochemistry

Volumn 46, Issue 24, 2007, Pages 7138-7145

  Devanathan, S ^a   Salamon, Z ^a   Tollin, G ^a   Fitch, J C ^a   Meyer, T E ^a   Berry, E A ^b   Cusanovich, M A ^a  

^a UNIVERSITY OF ARIZONA   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BINDING SITES; CONFORMATIONS; OPTICAL WAVEGUIDES; PHOSPHOLIPIDS; PLASMONS; SPECTROSCOPIC ANALYSIS;

PHOSPHOLIPID BILAYERS; PLASMON WAVEGUIDE RESONANCE; STIGMATELLIN;

PROTEINS;

CYTOCHROME B; CYTOCHROME C2; HEME; IRON SULFUR PROTEIN; STIGMATELLIN; UBIQUINOL CYTOCHROME C REDUCTASE;

ARTICLE; BINDING AFFINITY; BINDING SITE; DISSOCIATION CONSTANT; NONHUMAN; PHOSPHOLIPID BILAYER; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN METABOLISM; PROTEIN PROTEIN INTERACTION; RHODOBACTER CAPSULATUS; SPECTROSCOPY;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CYTOCHROMES C2; ELECTRON TRANSPORT COMPLEX III; IRON-SULFUR PROTEINS; KINETICS; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RHODOBACTER CAPSULATUS; SURFACE PLASMON RESONANCE;

RHODOBACTER CAPSULATUS;

EID: 34250871643     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602649u     Document Type: Article

References (38)

1. Deisenhofer, J., Epp, O., Miki, K., Huber, R., and Michel, H. (1985) Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution, Nature 318, 618-624.
2. 2+) interactions, Proc. Natl. Acad. Sci. U.S.A. 85, 8487-8491.
3. 1 complex from bovine heart mitochondria, Science 277, 60-66.
4. 1, Nature 392, 677-684.
5. 1 complex: Role of the iron sulfur protein and its mobility, Biochemistry 38, 15791-15806.
6. 1: Comparison with its mitochondrial and chloroplast counterparts, Photosynth. Res. 81, 251-275.
7. 2 isolated from Rhodobacter capsulatus determined at 2.5 Å resolution, J. Mol. Biol. 220, 673-685.
8. 2 from Rhodobacter sphaeroides in three crystal forms, Acta Crystallogr. D50, 596-602.
9. 2: reaction center electron transfer complex from Rhodobacter sphaeroides, J. Mol. Biol. 319, 501-515.
10. 1 complex with its bound substrate cytochrome c, Proc. Natl. Acad. Sci. U.S.A. 99, 2800-2805.
11. 2 onto the bacterial reaction center, Biochemistry 41, 5807-5815.
12. 2 and photosynthetic reaction center from Rhodobacter sphaeroides: changes in binding affinity and electron transfer rate due to mutation of interfacial hydrophobic residues are strongly correlated, Biochemistry 42, 14492-14500.
13. 2 and the photosynthetic reaction center from Rhodobacter sphaeroides: effects of charge modifying mutations on binding and electron transfer, Biochemistry 40, 8452-8462.
14. Rosen, D., Okamura, M. Y., and Feher, G. (1980) Interaction of cytochrome c with reaction centers of Rhodopseudomonas sphaeroides R-26: determination of number of binding sites and dissociation constants by equilibrium dialysis, Biochemistry 19, 5687-5692.
15. 2 hinge mutants, Biochemistry 43, 7717-7724.
16. 2 to photosynthetic reaction centers: Plasmon waveguide resonance spectroscopy, Biochemistry 43, 16405-16415.
17. 1 and cytochrome c, Photosynth. Res. 82, 1-16.
18. 1 complex, Biochemistry 42, 2816-2824.
19. Darrouzet, E., Valkova-Valchanova, M., Moser, C. C., and Dutton, P. L., and Daldal, F. (2000) Uncovering the [2Fe2S] domain movement in cytochrome BC1 and its implications for energy conversion, Proc. Natl. Acad. Sci. U.S.A. 97, 4567-4572.
20. Valkova-Valchonova, M., Darrouzet, E., Moomaw, C. R., Slaughter, C. A., and Daldal, F. (2000) Proteolytic cleavage of the Fe-S subunit hinge region of Rhodobacter capsulatus BC1 complex: Effects of inhibitors and mutation, Biochemistry 39, 15484-15492.
21. Xiao, K., Yu, L., and Yu, C. A. (2000) Confirmation of the involvement of protein domain movement during the catalytic cycle of the cytochrome BC1 complex by the formation of an intersubunit disulfide bond between cytochrome B and the iron-sulfur protein, J. Biol. Chem. 275, 38592-38604.
22. Bowman, M. K., Berry, E. A., Roberts, E. A., and Kramer, D. M. (2004) Orientation of the g-tensor axes of the Rieske subunit in the cytochrome BC1 complex, Biochemistry 43, 430-436.
23. Covian R., and Trumpower B. L. (2006) Regulatory interaction between ubiquinol oxidation and ubiquinone reduction sites in the dimeric cytochrome BC1 complex, J. Biol. Chem. 281, 30925-30932.
24. Andrews, K. M., Crofts, A. R., and Gennis, R. B. (1990) Large-scale purification and characterization of a highly active four-subunit cytochrome BC1 complex from Rhodobacter sphaeroides, Biochemistry 29, 2645-2651.
25. Ljungdahl, P. O., Pennoyer, J. D., Robertson, D. E., and Trumpower, B. L. (1987) Purification of highly active cytochrome BC1 complexes from phylogenetically diverse species by a single chromatographic procedure, Biochim. Biophys. Acta 891, 227-241.
26. Salamon, Z., Brown, M. F., and Tollin, G. (1999) Plasmon resonance spectroscopy: probing interactions within membranes. Trends Biochem. Sci. 24, 213-219.
27. Salamon, Z., and Tollin, G. (1996) Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. II. Binding of cytochrome c to oxidase containing cardiolipin/phosphatidylcholine membranes, Biophys. J. 71, 858-867.
28. Salamon, Z., Macleod, H. A., and Tollin, G. (1997) Coupled plasmon-waveguide resonators: a new spectroscopic tool for probing proteolipid film structure and properties, Biophys. J. 73, 2791-2797.
29. Salamon, Z., and Tollin, G. (2001) Plasmon resonance spectroscopy: probing molecular interactions at surfaces and interfaces, Spectroscopy 15, 161-175.
30. Esser, L., Gong, X., Yang, S., Yu, L., Yu, C. A., and Xia, D. (2006) Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome BC1 complex, Proc. Natl. Acad. Sci. U.S.A. 103, 13045-13050.
31. Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., and Jap, B. K. (1998) Complete structure of the 11-subunit bovine mitochondrial cytochrome BC1 complex, Science 281, 64-71.
32. Alves, I. D., Cowell, S. M., Salamon, Z., Devanathan, S., Tollin, G., and Hruby, V. J. (2004) Different structural states of the proteolipid membrane are produced by ligand binding to the human delta opioid receptor as shown by plasmon-waveguide resonance spectroscopy, Mol. Pharmacol. 65, 1248-1257.
33. Salamon, Z., Cowell, S., Varga, E., Yamamura, H. I., Hruby, V. J., and Tollin, G. (2000) Plasmon resonance studies of agonist/antagonist binding to the human delta-opioid receptor: new structural insights into receptor-ligand interactions, Biophys. J. 79, 2463-2474.
34. 1 complex through disulfide anchoring of a loop and β-branched amino acid near the heme-ligating methionine, Biochemistry 40, 14547-14556.
35. 2, Biochim. Biophys. Acta 430, 197-208.
36. 2 oxidoreductase activity from Rhodopseudomonas sphaeroides GA, Eur. J. Biochem. 126, 105-111.
37. 1 complex in the photosynthetic purple bacteria Rhodobacter capsulatus and Rhodopseudomonas viridis. Biochemistry 32, 4793-4800.
38. Kubota, T., Yoshikawa, S., and Matsubara, H. (1992) Kinetic mechanism of beef heart ubiquinol: Cytochrome c oxidoreductase, J. Biochem. 111, 91-98.