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Steric Control of the Hi‐CO MoFe Nitrogenase Complex Revealed by Stopped‐Flow Infrared Spectroscopy
Author(s) -
Yang ZhiYong,
Seefeldt Lance C.,
Dean Dennis R.,
Cramer Stephen P.,
George Simon J.
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201005145
Subject(s) - steric effects , azotobacter vinelandii , chemistry , nitrogenase , infrared spectroscopy , ligand (biochemistry) , infrared , spectroscopy , stereochemistry , crystallography , biochemistry , physics , organic chemistry , receptor , nitrogen fixation , nitrogen , quantum mechanics , optics
Revealing kinetics : For the α‐70 residue of MoFe nitrogenase in Azotobacter vinelandii the impact of substitution on the CO coordination to the enzyme's active center was studied by using stopped‐flow IR spectroscopy. The results suggest that in all cases the CO ligand binds to the Fe 2‐3‐6‐7 face of the FeMo‐cofactor (see picture).