Possible Roles of Two Quinone Molecules in Direct and Indirect Proton Pumps of Bovine Heart NADH-Quinone Oxidoreductase (Complex I)

Department

Molecular and Cellular Biology

Document Type

Article

Publication Date

12-2010

Abstract

In many energy transducing systems which couple electron and proton transport, for example, bacterial photosynthetic reaction center, cytochrome bc1-complex (complex III) and E. coli quinol oxidase (cytochrome bo3 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 SQNf (fast relaxing semiquinone) and SQNs (slow relaxing semiquinone). It was proposed that QNf serves as a "direct" proton carrier in the semiquinone-gated proton pump (Ohnishi and Salerno, FEBS Letters 579 (2005) 4555), while QNs works as a converter between one-electron and two-electron transport processes. This communication presents a revised hypothesis in which QNf plays a role in a "direct" redox-driven proton pump, while QNs triggers an "indirect" conformation-driven proton pump. QNf and QNs together serve as (1e−/2e−) converter, for the transfer of reducing equivalent to the Q-pool.

Journal Title

Biochimica et Biophysica Acta (BBA) - Bioenergetics

Journal ISSN

0006--3002

Volume

1797

Issue

12

First Page

1891

Last Page

1893

Digital Object Identifier (DOI)

10.1016/j.bbabio.2010.06.010

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