Novel cyanide inhibition at cytochrome c1 of Rhodobacter capsulatus cytochrome bc1

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1655, Issue 1-3, 2004, Pages 71-76

  Osyczka, Artur ^a,b   Moser, Christopher C ^a   Dutton, P Leslie ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b JAGIELLONIAN UNIVERSITY   (Poland)

Author keywords

CN; Cyanide; Cyanide inhibition; Cyt c1 CN; Cytochrome bc1; Cytochrome c1 with bound cyanide; Electron transfer; Heme; Qo and Qi sites; Rhodobacter capsulatus

Indexed keywords

1,4 BENZOQUINONE; CYANIDE; CYTOCHROME C1; HEME DERIVATIVE; UBIQUINOL CYTOCHROME C REDUCTASE;

ARTICLE; BACTERIUM; BINDING AFFINITY; BINDING SITE; CATALYSIS; ELECTRON TRANSPORT; ENERGY TRANSFER; MOLECULAR INTERACTION; NONHUMAN; OXIDATION REDUCTION REACTION; PHOTOSYNTHESIS; PRIORITY JOURNAL; RHODOBACTER CAPSULATUS; STEADY STATE; TURNOVER TIME;

BACTERIA (MICROORGANISMS); PHOTOBACTERIA; RHODOBACTER; RHODOBACTER CAPSULATUS;

EID: 1942504839     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.07.005     Document Type: Review

References (24)

1. 1 complex. Methods Enzymol. 126:1986;253-271.
2. Link T.A., Haase U., Brandt U., von Jagov G. What information do inhibitors provide about the structure of the hydroquinone oxidation site of ubihydroquinone: cytochrome c oxidoreductase. J. Bioenerg. Biomembranes. 1993;221-232.
3. 1 complex from bovine heart mitochondria. Science. 277:1997;60-66.
4. 1. Nature. 392:1998;677-684.
5. 1 complex. Science. 281:1998;64-71.
6. v fragment. Structure. 8:2000;669-684.
7. 1 complex from bovine heart. Proc. Natl. Acad. Sci. U. S. A. 95:1998;8026-8033.
8. 1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition. Biochemistry. 41:2002;11692-11702.
9. Proshlyakov D.A., Pressler M.A., Babcock G.T. Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase. Proc. Natl. Acad. Sci. U. S. A. 95:1998;8020-8025.
10. 1 complex and for photosynthetic growth of Rhodobacter capsulatus. Proc. Natl. Acad. Sci. U. S. A. 88:1991;492-496.
11. o) site with purified Fe-S protein subunit. Biochemistry. 37:1998;16242-16251.
12. Viola F., Aime S., Coletta M., Desideri A., Fasano M., Paoletti S., Tarricone C., Ascenzi P. Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse cytochrome c and to its carboxymethylated derivative: a comparative study. J. Inorg. Biochem. 62:1996;213-222.
13. 2 oxidoreductase from Rhodobacter capsulatus: definition of a minimal, functional isolated preparation. Biochemistry. 32:1993;1310-1317.
14. 2. J. Biol. Chem. 273:1998;25647-25653.
15. Dumortier C., Meyer T.E., Cusanovich M.A. Protein dynamics: imidazole binding to class I C-type cytochromes. Arch. Biochem. Biophys. 371:1999;142-148.
16. 1 complex through disulfide anchoring of a loop and a β-branched amino acid near the heme-ligating methionine. Biochemistry. 40:2001;14547-14556.
17. Schejter A., Aviram I. The reaction of cytochrome c with imidazole. Biochemistry. 8:1969;149-153.
18. Sutin N., Yandell J.K. Mechanisms of the reactions of cytochrome c. J. Biol. Chem. 247:1972;6932-6936.
19. 2 from Rhodobacter sphaeroides in three crystal forms. Acta Crystallogr. D50:1994;596-602.
20. Cohen D.J., King B.C., Hawkridge F.M. Spectroelectrochemical and electrochemical determination of ligand binding and electron transfer properties of myoglobin, cyanomyoglobin, and imidazolemyoglobin. J. Electroanal. Chem. 447:1998;53-62.
21. Meunier B., Rich P.R. Photolysis of the cyanide adduct of ferrous horseradish peroxidase. Biochim. Biophys. Acta. 1318:1997;235-245.
22. Mitchell R., Moody A.J., Rich P.R. Cyanide and carbon monoxide binding to the reduced form of cytochrome bo from Escherichia coli. Biochemistry. 1995:1995;7576-7585.
23. 1 complex. Biochemistry. 39:2000;4231-4236.
24. Moser C.C., Page C.C., Cogdell R.J., Barber J., Wraight C.A., Dutton P.L. Length, time, and energy scales of photosystems. Adv. Protein Chem. 63:2003;71-109.