An Fe 2 IV O 2 Diamond Core Structure for the Key Intermediate Q of Methane Monooxygenase-Reference-Cited by-同舟云学术

An Fe 2 IV O 2 Diamond Core Structure for the Key Intermediate Q of Methane Monooxygenase

Published:1997-01-24 Issue:5299 Volume:275 Page:515-518
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Shu Lijin¹,Nesheim Jeremy C.²,Kauffmann Karl³,Münck Eckard³,Lipscomb John D.²,Que Lawrence¹

Affiliation:

1. L. Shu and L. Que Jr., Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, MN 55455, USA.

2. J. C. Nesheim and J. D. Lipscomb, Department of Biochemistry, Medical School, and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, MN 55455, USA.

3. K. Kauffmann and E. Münck, Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA 15213, USA.

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 Fe 2 (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 Fe 2 IV O 2 diamond core.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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