Electroneutral and electrogenic catalysis by dihaem-containing succinate:quinone oxidoreductases.
Membrane protein complexes can support both the generation and utilization of a transmembrane electrochemical proton potential (Deltap), either by supporting transmembrane electron transfer coupled to protolytic reactions on opposite sides of the membrane or by supporting transmembrane proton transfer. Regarding the first mechanism, this has been unequivocally demonstrated to be operational for Deltap-dependent catalysis of succinate oxidation by quinone in the case of the dihaem-containing SQR (succinate:menaquinone reductase) from the Gram-positive bacterium Bacillus licheniformis. This is physiologically relevant in that it allows the transmembrane Deltap to drive the endergonic oxidation of succinate by menaquinone by the dihaem-containing SQR of Gram-positive bacteria. In the case of a related but different respiratory membrane protein complex, the dihaem-containing QFR (quinol:fumarate reductase) of the epsilon-proteobacterium Wolinella succinogenes, evidence has been obtained indicating that both mechanisms are combined, so as to facilitate transmembrane electron transfer by proton transfer via a both novel and essential compensatory transmembrane proton transfer pathway ('E-pathway'). This is necessary because, although the reduction of fumarate by menaquinol is exergonic, it is obviously not exergonic enough to support the generation of a Deltap. This compensatory E-pathway appears to be required by all dihaem-containing QFR enzymes and the conservation of the essential acidic residue on transmembrane helix V (Glu-C180 in W. succinogenes QFR) is a useful key for the sequence-based discrimination of these QFR enzymes from the dihaem-containing SQR enzymes.
Lancaster
C Roy D
CR
Cluster of Excellence "Macromolecular Complexes", Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, Max-von-Laue-Strasse 3, D-60438 Frankfurt am Main, Germany. Roy.Lancaster@structural-biology.eu
Herzog
Elena
E
Juhnke
Hanno D
HD
Madej
M Gregor
MG
Müller
Florian G
FG
Paul
Rajsekhar
R
Schleidt
Philipp G
PG
D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D004563:Electrochemistry; D004579:Electron Transport; D042963:Electron Transport Complex II / Q000737:chemistry / Q000378:metabolism*; D005650:Fumarates / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D011522:Protons; D011809:Quinones / Q000737:chemistry / Q000378:metabolism; D016968:Wolinella / Q000201:enzymology
D001426:Bacterial Proteins; D005650:Fumarates; D009097:Multienzyme Complexes; D011522:Protons; D011809:Quinones; C032005:fumaric acid; D010088:Oxidoreductases; D042963:Electron Transport Complex II; C424907:quinol fumarate reductase