Oxidation of methylamine by a Paracoccus denitrificans mutant impaired in the synthesis of the bc1 complex and the aa3-type oxidase. Evidence for the existence of an alternative cytochrome c oxidase in this bacterium.
A Paracoccus denitrificans fbcC-ctaDII double mutant strain impaired in the synthesis of both the bc1 complex and the aa3-type oxidase has been constructed. This mutant strain, which is still able to grow on methylamine as sole carbon and energy source, exhibits unimpaired oxygen consumption with succinate, methylamine and endogenous substrates as electron donors. From kinetic studies of the oxidation and reduction rates of cytochromes c, it can be concluded that P. denitrificans contains a second cytochrome c oxidase, different from the aa3-type.
De Gier
J W
JW
Vrije Universiteit, Department of Microbiology, Amsterdam, The Netherlands.
Van Spanning
R J
RJ
Oltmann
L F
LF
Stouthamer
A H
AH
D014450:Electron Transport Complex III / Q000096:biosynthesis* / Q000235:genetics; D003576:Electron Transport Complex IV / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D005798:Genes, Bacterial; D007700:Kinetics; D008744:Methylamines / Q000378:metabolism*; D009154:Mutation; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D010231:Paracoccus denitrificans / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity
D008744:Methylamines; C027451:methylamine; D003576:Electron Transport Complex IV; D014450:Electron Transport Complex III