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

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

doi:10.1126/science.abe5481

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

John W. Peters^*, Oliver Einsle^*, Dennis R. Dean, Serena DeBeer, Brian M. Hoffman, Patrick L. Holland, Lance C. Seefeldt

^*Corresponding author for this work

Chemistry

Research output: Contribution to journal › Review article › peer-review

32 Scopus citations

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.

Original language	English (US)
Article number	eabe5481
Journal	Science
Volume	371
Issue number	6530
DOIs	https://doi.org/10.1126/science.abe5481
State	Published - Feb 12 2021

Funding

Supported by NIH grants GM138592 (J.W.P.), GM111097 (B.M.H.), and GM-065313 (P.L.H.); U.S. Department of Energy, Office of Science, Basic Energy Sciences grants DE-SC0018143(J.W.P.),DE-SC0010834(D.R.D.), and DE-SC0010687(L.C.S.); NSF grant MCB-1908587(B.M.H.); Deutsche Forschungsgemeinschaft, PP 1927, project no. 311061829 (O.E.); and the Max Planck Society (S.D.) Author contributions: J.W.P. and O.E. coordinated the analysis and interpretation providing the basis for the comment; J.W.P., O.E., D.R.D., S.D., B.M.H., P.L.H., and L.C.S. provided contextual content and contributed to the preparation of the narrative. Competing interests: The authors declare no competing financial or nonfinancial interests.

ASJC Scopus subject areas

General

Access to Document

10.1126/science.abe5481

Cite this

@article{3506020da85d45b7967c8ba75c1ab105,

title = "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.",

author = "Peters, \{John W.\} and Oliver Einsle and Dean, \{Dennis R.\} and Serena DeBeer and Hoffman, \{Brian M.\} and Holland, \{Patrick L.\} and Seefeldt, \{Lance C.\}",

note = "Funding Information: Supported by NIH grants GM138592 (J.W.P.), GM111097 (B.M.H.), and GM-065313 (P.L.H.); U.S. Department of Energy, Office of Science, Basic Energy Sciences grants DE-SC0018143(J.W.P.),DE-SC0010834(D.R.D.), and DE-SC0010687(L.C.S.); NSF grant MCB-1908587(B.M.H.); Deutsche Forschungsgemeinschaft, PP 1927, project no. 311061829 (O.E.); and the Max Planck Society (S.D.) Author contributions: J.W.P. and O.E. coordinated the analysis and interpretation providing the basis for the comment; J.W.P., O.E., D.R.D., S.D., B.M.H., P.L.H., and L.C.S. provided contextual content and contributed to the preparation of the narrative. Competing interests: The authors declare no competing financial or nonfinancial interests. Publisher Copyright: Copyright {\textcopyright} 2021, American Association for the Advancement of Science",

year = "2021",

month = feb,

day = "12",

doi = "10.1126/science.abe5481",

language = "English (US)",

volume = "371",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "6530",

}

TY - JOUR

T1 - Comment on Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase

AU - Peters, John W.

AU - Einsle, Oliver

AU - Dean, Dennis R.

AU - DeBeer, Serena

AU - Hoffman, Brian M.

AU - Holland, Patrick L.

AU - Seefeldt, Lance C.

N1 - Funding Information: Supported by NIH grants GM138592 (J.W.P.), GM111097 (B.M.H.), and GM-065313 (P.L.H.); U.S. Department of Energy, Office of Science, Basic Energy Sciences grants DE-SC0018143(J.W.P.),DE-SC0010834(D.R.D.), and DE-SC0010687(L.C.S.); NSF grant MCB-1908587(B.M.H.); Deutsche Forschungsgemeinschaft, PP 1927, project no. 311061829 (O.E.); and the Max Planck Society (S.D.) Author contributions: J.W.P. and O.E. coordinated the analysis and interpretation providing the basis for the comment; J.W.P., O.E., D.R.D., S.D., B.M.H., P.L.H., and L.C.S. provided contextual content and contributed to the preparation of the narrative. Competing interests: The authors declare no competing financial or nonfinancial interests. Publisher Copyright: Copyright © 2021, American Association for the Advancement of Science

PY - 2021/2/12

Y1 - 2021/2/12

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/85101356633

UR - https://www.scopus.com/inward/citedby.url?scp=85101356633&partnerID=8YFLogxK

U2 - 10.1126/science.abe5481

DO - 10.1126/science.abe5481

M3 - Review article

C2 - 33574183

AN - SCOPUS:85101356633

SN - 0036-8075

VL - 371

JO - Science

JF - Science

IS - 6530

M1 - eabe5481

ER -