An Fe 2 IV O 2 Diamond Core Structure for the Key Intermediate Q of Methane Monooxygenase
- 24 January 1997
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 275 (5299) , 515-518
- https://doi.org/10.1126/science.275.5299.515
Abstract
A new paradigm for oxygen activation is required for enzymes such as methane monooxygenase (MMO), for which catalysis depends on a nonheme diiron center instead of the more familiar Fe-porphyrin cofactor. On the basis of precedents from synthetic diiron complexes, a high-valent Fe2(μ-O)2 diamond core has been proposed as the key oxidizing species for MMO and other nonheme diiron enzymes such as ribonucleotide reductase and fatty acid desaturase. The presence of a single short Fe-O bond (1.77 angstroms) per Fe atom and an Fe-Fe distance of 2.46 angstroms in MMO reaction intermediate Q, obtained from extended x-ray absorption fine structure and Mössbauer analysis, provides spectroscopic evidence that the diiron center in Q has an Fe2IVO2 diamond core.Keywords
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