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

John W. Peters | Zendy; Oliver Einsle | Zendy; Dennis R. Dean | Zendy; Serena DeBeer | Zendy; Brian M. Hoffman | Zendy; Patrick L. Holland | Zendy; Lance C. Seefeldt | Zendy

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

Author(s) -

John W. Peters,

Oliver Einsle,

Dennis R. Dean,

Serena DeBeer,

Brian M. Hoffman,

Patrick L. Holland,

Lance C. Seefeldt

Publication year - 2021

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.abe5481

Subject(s) - nitrogenase , reduction (mathematics) , cofactor , crystallography , chemistry , nitrogen fixation , enzyme , biochemistry , mathematics , nitrogen , geometry , organic chemistry

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.

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