جهت دسترسی به کاربرگه ی زیر، از این لینک استفاده کنید. http://dl.pgu.ac.ir/handle/10722/167628
Title: Oxidation of ultrafast radical clock substrate probes by the soluble methane monooxygenase from Methylococcus capsulatus (Bath)
Keywords: Binding Sites;Catalysis;Free Radicals;Kinetics;Methylococcaceae - Enzymology;Molecular Probes;Oxidation-Reduction;Oxygenases - Metabolism;Solubility;Substrate Specificity
Publisher: American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/;United States
Description: 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 radical and cationic intermediates. Oxidation of these substrates by a reconstituted sMMO system resulted in no rearranged products, allowing an upper limit of 150 fs to be placed on the lifetime of a putative radical species. This limit strongly suggests that there is no such substrate radical intermediate. The two enantiomers of trans-1-methyl-2- phenylcyclopropane were prepared, and the regioselectivity of their oxidation to the corresponding cyclopropylmethanol and cyclopropylphenol products was determined. The results are consistent with selective orientation of the two enantiomeric substrates in the hydrophobic cavity at the active site of sMMO, specific models for which were examined by molecular modeling.;link_to_OA_fulltext
Other Identifiers: Journal Of Biological Chemistry, 1999, v. 274 n. 16, p. 10771-10776
10.1074/jbc.274.16.10771
10776
WOS:000079751900018
0021-9258
16
10196150
eid_2-s2.0-0033574674
10771
http://hdl.handle.net/10722/167628
274
Type Of Material: Article
Appears in Collections:Department of Chemistry

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