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Frontispiece: Structural and Mechanistic Insights into CO 2 Activation by Nitrogenase Iron Protein
Author(s) -
Rettberg Lee A.,
Stiebritz Martin T.,
Kang Wonchull,
Lee Chi Chung,
Ribbe Markus W.,
Hu Yilin
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201985763
Subject(s) - nitrogenase , moiety , chemistry , stereochemistry , crystallography , reaction mechanism , kinetics , catalysis , biochemistry , nitrogen fixation , organic chemistry , nitrogen , physics , quantum mechanics
Proposed mechanism of binding, activation, and reduction of CO 2 by the nitrogenase Fe protein. CO 2 is initially captured by the concerted action of a conserved Arg pair. The further movement of the proximal Arg concomitant with a structural rearrangement of the [Fe 4 S 4 ] cluster results in the activation of CO 2 . Subsequently, a C−O bond is cleaved upon removal of the O atom as H 2 O, followed by release of the remaining CO moiety as the product of the reaction. For more information, see the Communication by M. W. Ribbe and Y. Hu et al. on page 13078 ff.