Intermediate P* from Soluble Methane Monooxygenase Contains a Diferrous Cluster
نویسندگان
چکیده
منابع مشابه
Substrate Specificity of Soluble Methane Monooxygenase
ion or by sequential loss of a *-bond electron and a proton termed an aborted epoxidation by Ortiz de Montellano (1986) and indeed epoxidated products are generated by methane monooxygenase from these substrates (Table 111). Oxidation of Cyclopropylbenzem-Attaching a cyclopropyl ring to the hydroxylated carbon atom of a hydrocarbon substrate as a means of testing for the presence of carbon radi...
متن کاملElectron Transfer Control in Soluble Methane Monooxygenase
The hydroxylation or epoxidation of hydrocarbons by bacterial multicomponent monooxygenases (BMMs) requires the interplay of three or four protein components. How component protein interactions control catalysis, however, is not well understood. In particular, the binding sites of the reductase components on the surface of their cognate hydroxylases and the role(s) that the regulatory proteins ...
متن کاملDioxygen activation in soluble methane monooxygenase.
The controlled oxidation of methane to methanol is a chemical transformation of great value, particularly in the pursuit of alternative fuels, but the reaction remains underutilized industrially because of inefficient and costly synthetic procedures. In contrast, methane monooxygenase enzymes (MMOs) from methanotrophic bacteria achieve this chemistry efficiently under ambient conditions. In thi...
متن کاملThe soluble methane monooxygenase gene cluster of the trichloroethylene-degrading methanotroph Methylocystis sp. strain M.
In methanotrophic bacteria, methane is oxidized to methanol by the enzyme methane monooxygenase (MMO). The soluble MMO enzyme complex from Methylocystis sp. strain M also oxidizes a wide range of aliphatic and aromatic compounds, including trichloroethylene. In this study, heterologous DNA probes from the type II methanotroph Methylosinus trichosporium OB3b were used to isolate souble MMO (sMMO...
متن کاملStructure of the soluble methane monooxygenase regulatory protein B.
The soluble methane monooxygenase (sMMO; EC 1.14.13.25) from the pseudothermophile Methylococcus capsulatus (Bath) is a three-component enzyme system that catalyzes the selective oxidation of methane to methanol. We have used NMR spectroscopy to produce a highly refined structure of MMOB, the 16-kDa regulatory protein of this system. This structure has a unique and intricate fold containing sev...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemistry
سال: 2013
ISSN: 0006-2960,1520-4995
DOI: 10.1021/bi400182y