English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  DetailsSummary

Released
Journal Article

Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism [Review]

MPS-Authors
/persons/resource/persons137603

Biel,  S.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137768

Lancaster,  C. R D.
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Kröger, A., Biel, S., Simon, J., Gross, R., Unden, G., & Lancaster, C. R. D. (2002). Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism [Review]. Biochimica et Biophysica Acta - Bioenergetics, 1553(1-2), 23-38.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DC78-F
Abstract
Wolinella succinogenes performs oxidative phosphorylation with fumarate instead of O-2 as terminal electron acceptor and H-2 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 H-2 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. (C) 2002 Elsevier Science B.V. All rights reserved. [References: 67]