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Comment on "Structural evidence for a dynamic metallocofactor during N₂ reduction by Mo-nitrogenase".

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 N₂ or an N₂-derived species to the active-site FeMo cofactor. Independent refinement of the structure and consideration of biochemical evidence do not support this claim.

SUBMITTER: Peters JW

PROVIDER: S-EPMC7931246 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

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Comment on "Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase".

Peters John W JW Einsle Oliver O Dean Dennis R DR DeBeer Serena S Hoffman Brian M BM Holland Patrick L PL Seefeldt Lance C LC

Science (New York, N.Y.) 20210201 6530

Kang et al (Reports, 19 June 2020, p. 1381) report a structure of the nitrogenase MoFe protein that is interpreted to indicate binding of N2 or an N2-derived species to the active-site FeMo cofactor. Independent refinement of the structure and consideration of biochemical evidence do not support this claim. ...[more]

PMID: 33574183

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Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase.

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