Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State E2(2H), Assigned Using Cryogenic Intra Electron Paramagnetic Resonance Cavity Photolysis-Reference-Cited by-同舟云学术

Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State E2(2H), Assigned Using Cryogenic Intra Electron Paramagnetic Resonance Cavity Photolysis

Published:2018-03-24 Issue:12 Volume:57 Page:6847-6852
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Lukoyanov Dmitriy A.¹,Khadka Nimesh²,Yang Zhi-Yong²^ORCID,Dean Dennis R.³,Seefeldt Lance C.²^ORCID,Hoffman Brian M.¹^ORCID

Affiliation:

1. Departments of Chemistry and Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, United States

2. Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322, United States

3. Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061, United States

Funder

Basic Energy Sciences

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acs.inorgchem.8b00271

Reference26 articles.

1. Mechanism of Molybdenum Nitrogenase

2. Duplication and extension of the Thorneley and Lowe kinetic model for Klebsiella pneumoniae nitrogenase catalysis using a mathematica software platform

3. Reductive Elimination of H2 Activates Nitrogenase to Reduce the N≡N Triple Bond: Characterization of the E4(4H) Janus Intermediate in Wild-Type Enzyme

4. Is Mo Involved in Hydride Binding by the Four-Electron Reduced (E4) Intermediate of the Nitrogenase MoFe Protein?

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