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 Molybdenum Enzymes, Cofactors, and Model Systems, 535 . pp. 170-185. ISSN 0097-6156
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Official URL: http://doi.org/10.1021/bk-1993-0535.ch011
Related URL: http://dx.doi.org/10.1021/bk-1993-0535.ch011
Abstract
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 α2β2 tetramer, where the homologous α and β 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 αβ subunit interface. Docking studies between the iron protein and molybdenum iron protein suggest a possible interaction mode between these two proteins.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to American Chemical Society |
| ID Code: | 129109 |
| Deposited On: | 08 Nov 2022 10:00 |
| Last Modified: | 08 Nov 2022 10:00 |
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