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The mechanism of methane and dioxygen activation in the catalytic cycle of methane monooxygenase
Author(s) -
Shteinman Albert A.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00195-f
Subject(s) - methane monooxygenase , methane , chemistry , mechanism (biology) , catalysis , monooxygenase , catalytic cycle , photochemistry , biochemistry , organic chemistry , enzyme , physics , cytochrome p450 , quantum mechanics
The binuclear structure of the active center of methane monooxygenase plays a determining role in dioxygen activation and in selectivity and specificity of alkane oxidation with this enzyme. A new mechanism is suggested for binding and activation of O 2 , which involves side‐on binding of O 2 2− to iron atoms followed by its conversion to the bis‐μ‐oxo complex considered as an alternative of ferryl in CH 4 activation. This mechanism results in the sequence of the cleavage of the O—O bond of peroxide O/O 2− instead of the opposite sequence O 2− /O, which takes place in the case of heme monooxygenase cytochrome P ‐450. Therefore, in this case there is no necessity of the charge relay system [N.B. Gerber and S.G. Sligar, J. Am. Chem. Soc. 114 (1992) 8742] for the transformation of O 2 to an active intermediate. The experiment for checking this hypothesis is suggested.