[Role of CO-binding cytochrome c in enzymatic oxidation of methane by the bacterium Methylococcus capsulatus].
The cytochrome c spectrally related to cco cytochromes has been isolated and purified from the methane-oxidizing bacterium Methylococcus capsulatus. The cytochrome binds CO but does not bind other substrates of methane monooxygenase, does not activate the methane monooxygenase reaction and is not a component of methane monooxygenase. In the methanol dehydrogenase enzymatic system cytochrome cco functions as electron acceptor. A possible role of cytochrome cco as electron carrier intermediate in the sequence of the dehydrogenase and oxidase enzymatic systems of M. capsulatus is discussed.
D002248:Carbon Monoxide / Q000378:metabolism*; D003574:Cytochrome c Group / Q000378:metabolism*; D019605:Euryarchaeota / Q000378:metabolism*; D007700:Kinetics; D008697:Methane / Q000378:metabolism*; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding
D003574:Cytochrome c Group; D002248:Carbon Monoxide; D010105:Oxygenases; C021555:methane monooxygenase; D008697:Methane
Rol' tsitokhroma c, sviazyvaiushchego CO, v fermentativnom okislenii metana bakteriei Methylococcus capsulatus.