Crystal Structures of the Iron Protein and Molybdenum-Iron Protein of Nitrogenase

Rees, D. C., Kim, J., Georgiadis, M. M., Komiya, H., Chirino, A. J., Woo, D., Schlessman, J., Chan, M. K., Joshua-Tor, L., Santillan, G., Chakrabarti, P., Hsu, B. T. (1993) Crystal Structures of the Iron Protein and Molybdenum-Iron Protein of Nitrogenase. In: Molybdenum Enzymes, Cofactors, and Model Systems. ACS Symposium Series, 535 (535). American Chemical Society, pp. 170-185. ISBN 0-8412-2708-X

DOI: 10.1021/bk-1993-0535.ch011


Three-dimensional structures of the nitrogenase iron protein and molybdenum-iron protein from Azotobacter vinelandii have been determined by x-ray crystallography. The iron protein contains a single 4Fe:4S cluster symmetrically liganded by two identical subunits. The molybdenum-iron protein is an α2?2 tetramer, where the homologous α and ? subunits surround two different types of metal centers: the FeMo-cofactor and the P-cluster pair. Both centers are constructed from two bridged clusters; the FeMo-cofactor has 4Fe:3S and 1Mo:3Fe:3S cluster bridged by three non-protein ligands, while the P-cluster pair contains two 4Fe:4S clusters bridged by two cysteine ligands located at the α? subunit interface. Docking studies between the iron protein and molybdenum iron protein suggest a possible interaction mode between these two proteins.

Item Type: Book Section
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Joshua-Tor lab
Depositing User: CSHL Librarian
Date: 1993
Date Deposited: 20 Mar 2012 19:07
Last Modified: 17 Jan 2017 17:43

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving