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

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:

Peters John W.¹^ORCID,Einsle Oliver²^ORCID,Dean Dennis R.³^ORCID,DeBeer Serena⁴^ORCID,Hoffman Brian M.⁵^ORCID,Holland Patrick L.⁶^ORCID,Seefeldt Lance C.⁷^ORCID

Affiliation:

1. Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, USA.

2. Institute of Biochemistry, Albert-Ludwigs Universität, Freiburg, Germany.

3. Biochemistry Department, Virginia Tech, Blacksburg, VA 24061, USA.

4. Max Planck Institute for Chemical Energy Conversion, D-45470 Mülheim an der Ruhr, Germany.

5. Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.

6. Department of Chemistry, Yale University, New Haven, CT 06520, USA.

7. Chemistry and Biochemistry, Utah State University, Logan, UT 84322, USA.

Abstract

Kang et al . (Reports, 19 June 2020, p. 1381) report a structure of the nitrogenase MoFe protein that is interpreted to indicate binding of N 2 or an N 2 -derived species to the active-site FeMo cofactor. Independent refinement of the structure and consideration of biochemical evidence do not support this claim.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference11 articles.

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

2. Structural Enzymology of Nitrogenase Enzymes

3. Reduction of Substrates by Nitrogenases

4. The Spectroscopy of Nitrogenases

5. Redox-Dependent Structural Changes in the Nitrogenase P-Cluster,

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