Refinement of a Model for the Nitrogenase MoFe Cluster Using Single‐Crystal Mo and Fe EXAFS | Zendy

Cramer Stephen P. | Zendy; Chen Jie | Zendy; Christiansen Jason | Zendy; Campobasso Nino | Zendy; Bolin Jeffrey T. | Zendy; Tittsworth Roland C. | Zendy; Hales Brian J. | Zendy; Rehr John J. | Zendy

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Refinement of a Model for the Nitrogenase MoFe 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.

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