Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1655, Issue 1-3, Pages 71-76Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2003.07.005
Keywords
cytochrome bc(1); cyanide inhibition; heme; electron transfer; Rhodobacter capsulatus
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Funding
- NIGMS NIH HHS [GM-27309] Funding Source: Medline
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Oxidized cytochrome c(1) in photosynthetic bacterium Rhodobacter capsulatus cytochrome bc(1) reversibly binds cyanide with surprisingly high, micromolar affinity. The binding dramatically lowers the redox midpoint potential of heme c(1) and inhibits steady-state turnover activity of the enzyme. As cytochrome c(1), an auxiliary redox center of the high-potential chain of cytochrome bc(1), does not interact directly with the catalytic quinone/quinol binding sites Q(o) and Q(i), cyanide introduces a novel, Q-site independent locus of inhibition. This is the first report of a reversible inhibitor that manipulates the energetics and electron transfers of the high-potential redox chain of cytochrome bc(1), while maintaining quinone Substrate catalytic sites in an intact form. (C) 2004 Elsevier B.V. All rights reserved.
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