[Role of CO-binding cytochrome c in enzymatic oxidation of methane by the bacterium Methylococcus capsulatus]
- PMID: 6288124
[Role of CO-binding cytochrome c in enzymatic oxidation of methane by the bacterium Methylococcus capsulatus]
Abstract
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.
Similar articles
-
Three-dimensional structure determination of a protein supercomplex that oxidizes methane to formaldehyde in Methylococcus capsulatus (Bath).Biochemistry. 2006 Oct 3;45(39):11905-14. doi: 10.1021/bi061294p. Biochemistry. 2006. PMID: 17002291
-
Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane.Nature. 2005 Mar 10;434(7030):177-82. doi: 10.1038/nature03311. Epub 2005 Jan 26. Nature. 2005. PMID: 15674245
-
Bacterial oxidation of methane and methanol.Adv Microb Physiol. 1986;27:113-210. doi: 10.1016/s0065-2911(08)60305-7. Adv Microb Physiol. 1986. PMID: 3020939 Review. No abstract available.
-
[Electron transport chain in a thermophilic methane-oxidizing culture of Methylococcus thermophilus].Mikrobiologiia. 1981 Jan-Feb;50(1):13-20. Mikrobiologiia. 1981. PMID: 7012552 Russian.
-
Insights into the obligate methanotroph Methylococcus capsulatus.Trends Microbiol. 2005 May;13(5):195-8. doi: 10.1016/j.tim.2005.03.003. Trends Microbiol. 2005. PMID: 15866035 Review.