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Refinement of a Model for the Nitrogenase MoFe Cluster Using Single‐Crystal Mo and Fe EXAFS
Author(s) -
Cramer Stephen P.,
Chen Jie,
Christiansen Jason,
Campobasso Nino,
Bolin Jeffrey T.,
Tittsworth Roland C.,
Hales Brian J.,
Rehr John J.
Publication year - 1993
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199315921
Subject(s) - extended x ray absorption fine structure , nitrogenase , cluster (spacecraft) , crystallography , single crystal , crystal structure , chemistry , molybdenum , crystal (programming language) , materials science , spectral line , absorption spectroscopy , physics , inorganic chemistry , optics , computer science , programming language , organic chemistry , nitrogen fixation , astronomy , nitrogen
Increasingly precise structural information is available for the FeMo cofactor of nitrogenase. EXAFS spectra of a single crystal of nitrogenase from C. pasteurianum provided MoFe and FeFe distances shorter than those previously determined by X‐ray crystallography (2.7 vs. 2.9 Å and 2.61 vs. 2.83 Å, respectively). In addition, a long‐range MoFe interaction at 5.1 Å was found. These structural data allow the design of a model of the active center (picture on the right) that is more compact and symmetrical than that based on an X‐ray structure analysis having a resolution of 2.2 Å.