Response to Comment on “Structural evidence for a dynamic metallocofactor during N 2 reduction by Mo-nitrogenase”-Reference-Cited by-同舟云学术

Response to Comment on “Structural evidence for a dynamic metallocofactor during N 2 reduction by Mo-nitrogenase”

Published:2021-02-12 Issue:6530 Volume:371 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Kang Wonchull¹^ORCID,Lee Chi Chung¹^ORCID,Jasniewski Andrew J.¹^ORCID,Ribbe Markus W.¹²^ORCID,Hu Yilin¹^ORCID

Affiliation:

1. Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA.

2. Department of Chemistry, University of California, Irvine, CA 92697, USA.

Abstract

Peters et al . comment on our report of the dynamic structure of the nitrogenase metallocofactor during N 2 reduction. Their claim that their independent structural refinement and consideration of biochemical data contradict our finding is incorrect and is strongly refuted by our biochemical and structural data that collectively and conclusively point to the binding of dinitrogen species to the nitrogenase cofactor.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference9 articles.

1. Comment on “Structural evidence for a dynamic metallocofactor during N 2 reduction by Mo-nitrogenase”

2. Structural evidence for a dynamic metallocofactor during N 2 reduction by Mo-nitrogenase

3. A bound reaction intermediate sheds light on the mechanism of nitrogenase

4. Does the crystal structure of vanadium nitrogenase contain a reaction intermediate? Evidence from quantum refinement

5. QM/MM calculations reveal a bridging hydroxo group in a vanadium nitrogenase crystal structure

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