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J Bioenerg Biomembr. 2001 Jun;33(3):169-77.

Complex I: a chimaera of a redox and conformation-driven proton pump?

Author information

1
Institut für Biochemie, Universität Düsseldorf, Germany. Thorsten.Friedrich@uni-duesseldorf.de

Abstract

From phylogenetic sequence analysis, it can be concluded that the proton-pumping NADH:ubiquinone oxidoreductase (complex I) has evolved from preexisting modules for electron transfer and proton translocation. It is built up by a peripheral NADH dehydrogenase module, an amphipatic hydrogenase module, and a membrane-bound transporter module. These modules, or at least part of them, are also present in various other bacterial enzymes. It is assumed that they fulfill a similar function in complex I and related enzymes. Based on the function of the individual modules, it is possible to speculate about the mechanism of complex I. The hydrogenase module might work as a redox-driven proton pump, while the transporter module might act as a conformation-driven proton pump. This implies that complex I contains two energy-coupling sites. The NADH dehydrogenase module seems to be involved in electron transfer and not in proton translocation.

PMID:
11695826
[Indexed for MEDLINE]

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