Hydroxylation of Methane by Non-Heme Diiron Enzymes: Molecular Orbital Analysis of C−H Bond Activation by Reactive Intermediate Q-Reference-Cited by-同舟云学术

Hydroxylation of Methane by Non-Heme Diiron Enzymes: Molecular Orbital Analysis of C−H Bond Activation by Reactive Intermediate Q

Published:2002-11-15 Issue:49 Volume:124 Page:14608-14615
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Baik Mu-Hyun¹,Gherman Benjamin F.¹,Friesner Richard A.¹,Lippard Stephen J.¹

Affiliation:

1. Contribution from the Department of Chemistry, Columbia University, New York, New York 10027, and the Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja026794u

Reference85 articles.

1. Reactions of Non-Heme Iron(II) Centers with Dioxygen in Biology and Chemistry

2. Studies of the Soluble Methane Monooxygenase Protein System: Structure, Component Interactions, and Hydroxylation Mechanism

3. Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters

4. Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins

5. Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states

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