Is Mo Involved in Hydride Binding by the Four-Electron Reduced (E4) Intermediate of the Nitrogenase MoFe Protein?-Reference-Cited by-同舟云学术

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

Published:2010-02-01 Issue:8 Volume:132 Page:2526-2527
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lukoyanov Dmitriy¹,Yang Zhi-Yong¹,Dean Dennis R.¹,Seefeldt Lance C.¹,Hoffman Brian M.¹

Affiliation:

1. Department of Chemistry, Northwestern University, Evanston, Illinois 60208, Department of Biochemistry, Virginia Tech, Blacksburg, Virginia 24061, and Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja910613m

Reference20 articles.

1. Mechanism of Molybdenum Nitrogenase

2. Catalytic Reduction of Dinitrogen to Ammonia at a Single Molybdenum Center

3. Structure−Function Relationships of Alternative Nitrogenases

4. Localization of a Catalytic Intermediate Bound to the FeMo-cofactor of Nitrogenase

Cited by 80 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Water-catalyzed iron-molybdenum carbyne formation in bimetallic acetylene transformation;Nature Communications;2024-09-04

2. Terminal Hydride Complex of High-Spin Mn;Journal of the American Chemical Society;2024-06-28

3. Mysteries of metallome evolution: Integrating insights from the Earth and life sciences;Reference Module in Earth Systems and Environmental Sciences;2024

4. Nitrogenase beyond the Resting State: A Structural Perspective;Molecules;2023-12-05

5. How thermal fluctuations influence the function of the FeMo cofactor in nitrogenase enzymes;Chem Catalysis;2023-07