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Comment on "Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase".
Peters, John W; Einsle, Oliver; Dean, Dennis R; DeBeer, Serena; Hoffman, Brian M; Holland, Patrick L; Seefeldt, Lance C.
Afiliação
  • Peters JW; Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, USA. jw.peters@wsu.edu einsle@bio.chemie.uni-freiburg.de.
  • Einsle O; Institute of Biochemistry, Albert-Ludwigs Universität, Freiburg, Germany. jw.peters@wsu.edu einsle@bio.chemie.uni-freiburg.de.
  • Dean DR; Biochemistry Department, Virginia Tech, Blacksburg, VA 24061, USA.
  • DeBeer S; Max Planck Institute for Chemical Energy Conversion, D-45470 Mülheim an der Ruhr, Germany.
  • Hoffman BM; Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.
  • Holland PL; Department of Chemistry, Yale University, New Haven, CT 06520, USA.
  • Seefeldt LC; Chemistry and Biochemistry, Utah State University, Logan, UT 84322, USA.
Science ; 371(6530)2021 02 12.
Article em En | MEDLINE | ID: mdl-33574183
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Azotobacter vinelandii / Molibdoferredoxina Idioma: En Ano de publicação: 2021 Tipo de documento: Article
Texto completo
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PubMed Links
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Azotobacter vinelandii / Molibdoferredoxina Idioma: En Ano de publicação: 2021 Tipo de documento: Article