Possible roles of two quinone molecules in direct and indirect proton pumps of bovine heart NADH-quinone oxidoreductase (complex I)
- PMID: 20599678
- PMCID: PMC2997716
- DOI: 10.1016/j.bbabio.2010.06.010
Possible roles of two quinone molecules in direct and indirect proton pumps of bovine heart NADH-quinone oxidoreductase (complex I)
Abstract
In many energy transducing systems which couple electron and proton transport, for example, bacterial photosynthetic reaction center, cytochrome bc(1)-complex (complex III) and E. coli quinol oxidase (cytochrome bo(3) complex), two protein-associated quinone molecules are known to work together. T. Ohnishi and her collaborators reported that two distinct semiquinone species also play important roles in NADH-ubiquinone oxidoreductase (complex I). They were called SQ(Nf) (fast relaxing semiquinone) and SQ(Ns) (slow relaxing semiquinone). It was proposed that Q(Nf) serves as a "direct" proton carrier in the semiquinone-gated proton pump (Ohnishi and Salerno, FEBS Letters 579 (2005) 4555), while Q(Ns) works as a converter between one-electron and two-electron transport processes. This communication presents a revised hypothesis in which Q(Nf) plays a role in a "direct" redox-driven proton pump, while Q(Ns) triggers an "indirect" conformation-driven proton pump. Q(Nf) and Q(Ns) together serve as (1e(-)/2e(-)) converter, for the transfer of reducing equivalent to the Q-pool.
Copyright © 2010 Elsevier B.V. All rights reserved.
Figures
References
-
- Okamura MY, Paddock ML, Graige MS, Feher G. Proton and electron transfer in bacterial reaction centers. Biochim Biophys Acta. 2000;1458:148–163. - PubMed
-
- Mitchell P. Protonmotive redox mechanism of the cytochrome b-c1 complex in the respiratory chain: protonmotive ubiquinone cycle. FEBS Lett. 1975;56:1–6. - PubMed
-
- Croft AR. The cytochrome bc1 complex: Function in the context of structure. Annu. Rev. Physiol. 2004;66:689–733. - PubMed
-
- Sato-Watanabe M, Mogi T, Ogura T, Kitagawa T, Miyoshi H, Iwamura H, Anraku Y. Identification of a novel quinone-binding site in the cytochrome bo complex from Escherichia coli. J Biol Chem. 1994;269:28908–28912. - PubMed
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous
