6533b7d9fe1ef96bd126c369
RESEARCH PRODUCT
Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism.
Simone BielJörg SimonRoland GrossAchim KrögerGottfried UndenC. Roy D. Lancastersubject
HydrogenaseStereochemistryBiophysicsOxidative phosphorylationCoupling mechanismFormate dehydrogenaseBiochemistryCatalysisOxidative PhosphorylationWolinella succinogenesElectron Transportchemistry.chemical_compoundFumaratesHydrogenaseFormatechemistry.chemical_classificationFumarate respirationBinding SitesbiologySuccinate dehydrogenaseCell MembraneVitamin K 2Cell BiologyElectron acceptorFumarate reductaseElectron transport chainFormate DehydrogenasesWolinellaSuccinate DehydrogenaseBiochemistrychemistryModels Chemicalbiology.proteinFormate dehydrogenaseEnergy MetabolismOxidation-ReductionBacillus subtilisdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2002-01-23 | Biochimica et biophysica acta |