Format

Send to

Choose Destination
Biochim Biophys Acta. 2002 Jan 17;1553(1-2):23-38.

Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism.

Author information

1
Institüt für Mikrobiologie, Johann Wolfgang Goethe-Universität, Frankfurt am Main, Germany. a.kroeger@em.uni-frankfurt.de

Abstract

Wolinella succinogenes performs oxidative phosphorylation with fumarate instead of O2 as terminal electron acceptor and H2 or formate as electron donors. Fumarate reduction by these donors ('fumarate respiration') is catalyzed by an electron transport chain in the bacterial membrane, and is coupled to the generation of an electrochemical proton potential (Deltap) across the bacterial membrane. The experimental evidence concerning the electron transport and its coupling to Deltap generation is reviewed in this article. The electron transport chain consists of fumarate reductase, menaquinone (MK) and either hydrogenase or formate dehydrogenase. Measurements indicate that the Deltap is generated exclusively by MK reduction with H2 or formate; MKH2 oxidation by fumarate appears to be an electroneutral process. However, evidence derived from the crystal structure of fumarate reductase suggests an electrogenic mechanism for the latter process.

PMID:
11803015
DOI:
10.1016/s0005-2728(01)00234-1
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center