An Fe2/(IV)O2 diamond core structure for the key intermediate Q of methane monooxygenase

Lijin Shu, Jeremy C. Nesheim, Karl Kauffmann, Eckard Münck, John D Lipscomb, Larry Que

Research output: Contribution to journalArticlepeer-review

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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 Mossbauer analysis, provides spectroscopic evidence that the diiron center in Q has an Fe2/(IV)O2 diamond core.

Original languageEnglish (US)
Pages (from-to)515-518
Number of pages4
JournalScience
Volume275
Issue number5299
DOIs
StatePublished - Jan 24 1997

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