The cytochrome c reductase/oxidase respiratory pathway of Paracoccus denitrificans: genetic and functional studies.
Data are presented on three components of the quinol oxidation branch of the Paracoccus respiratory chain: cytochrome c reductase, cytochrome c552, and the a-type terminal oxidase. Deletion mutants in the bc1 and the aa3 complex give insight into electron pathways, assembly processes, and stability of both redox complexes, and, moreover, are an important prerequisite for future site-directed mutagenesis experiments. In addition, evidence for a role of cytochrome c552 in electron transport between complex III and IV is presented.
Steinrücke
P
P
Institute of Biochemistry, Medical University of Lübeck, Germany.
Gerhus
E
E
Jetzek
M
M
Turba
A
A
Ludwig
B
B
D003574:Cytochrome c Group / Q000235:genetics / Q000378:metabolism; D014450:Electron Transport Complex III / Q000235:genetics / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000235:genetics / Q000378:metabolism*; D009245:NADH Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D010231:Paracoccus denitrificans / Q000201:enzymology* / Q000235:genetics
D003574:Cytochrome c Group; C083951:cytochrome c553; C022302:cytochrome C-552; D009245:NADH Dehydrogenase; D003576:Electron Transport Complex IV; D014450:Electron Transport Complex III