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Structural models for the metal centers in the nitrogenase molybdenum-iron protein

Kim, Jongsun and Rees, D. C. (1992) Structural models for the metal centers in the nitrogenase molybdenum-iron protein. Science, 257 (5077). pp. 1677-1682. ISSN 0036-8075. doi:10.1126/science.1529354. https://resolver.caltech.edu/CaltechAUTHORS:20150122-144354973

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Abstract

Structural models for the nitrogenase FeMo-cofactor and P-clusters are proposed based on crystallographic analysis of the nitrogenase molybdenum-iron (MoFe)-protein from Azotobacter vinelandii at 2.7 angstrom resolution. Each center consists of two bridged clusters; the FeMo-cofactor has 4Fe:3S and 1Mo:3Fe:3S clusters bridged by three non-protein ligands, and the P-clusters contain two 4Fe:4S clusters bridged by two cysteine thiol ligands. Six of the seven Fe sites in the FeMo-cofactor appear to have trigonal coordination geometry, including one ligand provided by a bridging group. The remaining Fe site has tetrahedral geometry and is liganded to the side chain of Cys ^(α 275). The Mo site exhibits approximate octahedral coordination geometry and is liganded by three sulfurs in the cofactor, two oxygens from homocitrate, and the imidazole side chain of His^(α 442). The P-clusters are liganded by six cysteine thiol groups, two which bridge the two clusters, α88 and β95, and four which singly coordinate the remaining Fe sites, α62, α154, β70, and β153. The side chain of Ser^(β188) may also coordinate one iron. The polypeptide folds of the homologous α and β subunits surrounding the P-clusters are approximately related by a twofold rotation that may be utilized in the binding interactions between the MoFe-protein and the nitrogenase Fe-protein. Neither the FeMo-cofactor nor the P-clusters are exposed to the surface, suggesting that substrate entry, electron transfer, and product release must involve a carefully regulated sequence of interactions between the MoFe-protein and Fe-protein of nitrogenase.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1126/science.1529354DOIArticle
http://www.sciencemag.org/content/257/5077/1677PublisherArticle
http://www.jstor.org/stable/2880131JSTORArticle
ORCID:
AuthorORCID
Rees, D. C.0000-0003-4073-1185
Additional Information:© 1992 American Association for the Advancement of Science. 19 June 1992; Accepted 18 August 1992. Discussions with J. B. Howard, J. E. Bercaw, and H. B. Gray and the assistance of M. M. Georgiadis, B. T. Hsu, D. Woo, A. J. Chirino, H. Komiya, D. Malerba, and M. K. Chan are gratefully appreciated. Supported by NSF grant DMB91-18689, with instrumentation funded in part by the Beckman Institute and the Joseph Irvine Equipment fund.
Funders:
Funding AgencyGrant Number
NSFDMB91-18689
Caltech Beckman InstituteUNSPECIFIED
Joseph Irvine Equipment FundUNSPECIFIED
Issue or Number:5077
DOI:10.1126/science.1529354
Record Number:CaltechAUTHORS:20150122-144354973
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150122-144354973
Official Citation:Kim, J., & Rees, D. (1992). Structural models for the metal centers in the nitrogenase molybdenum-iron protein. Science, 257(5077), 1677-1682. doi: 10.1126/science.1529354
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:54003
Collection:CaltechAUTHORS
Deposited By: Joanne McCole
Deposited On:23 Jan 2015 02:21
Last Modified:10 Nov 2021 20:26

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