This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Methane monooxygenase
From Proteopedia
(Difference between revisions)
| Line 6: | Line 6: | ||
* Subunit α is the hydroxylase (MMOH) and contains the di-iron active site.<br /> | * Subunit α is the hydroxylase (MMOH) and contains the di-iron active site.<br /> | ||
* Subunit β is a reductase which contains the co-factors FAD and 2Fe-2S complex.<br /> | * Subunit β is a reductase which contains the co-factors FAD and 2Fe-2S complex.<br /> | ||
| - | * Subunit γ is regulatory ( | + | * Subunit γ is regulatory (MMOR) and is involved in coupling.<br /> |
MMO is found in methanotropic bacteria. | MMO is found in methanotropic bacteria. | ||
Revision as of 09:45, 6 September 2020
| |||||||||||
3D structures of methane monooxygenase
Updated on 06-September-2020
References
- ↑ Lipscomb JD. Biochemistry of the soluble methane monooxygenase. Annu Rev Microbiol. 1994;48:371-99. PMID:7826011 doi:http://dx.doi.org/10.1146/annurev.mi.48.100194.002103
- ↑ Miyaji A. Particulate methane monooxygenase from Methylosinus trichosporium OB3b. Methods Enzymol. 2011;495:211-25. doi: 10.1016/B978-0-12-386905-0.00014-0. PMID:21419924 doi:http://dx.doi.org/10.1016/B978-0-12-386905-0.00014-0

