Substrate specificity of soluble methane monooxygenase
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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...
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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 کاملOxidation of ultrafast radical clock substrate probes by the soluble methane monooxygenase from Methylococcus capsulatus (Bath).
Radical clock substrate probes were used to assess the viability of a discrete substrate radical species in the mechanism of hydrocarbon oxidation by the soluble methane monooxygenase (sMMO) from Methylococcus capsulatus (Bath). New substituted cyclopropane probes were used with very fast ring-opening rate constants and other desirable attributes, such as the ability to discriminate between rad...
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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)84627-6