Possible roles of two quinone molecules in direct and indirect proton pumps of bovine heart NADH-quinone oxidoreductase (complex I)
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. Oh...
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Published in | Biochimica et biophysica acta Vol. 1797; no. 12; pp. 1891 - 1893 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.12.2010
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 On leave of absence from the Philadelphia Biomedical Research Institute. |
ISSN: | 0005-2728 0006-3002 1879-2650 |
DOI: | 10.1016/j.bbabio.2010.06.010 |