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The Nitrogenase FeMo-Cofactor and P-Cluster pair: 2.2 Å Resolution Structures
Abstract
Structures recently proposed for the FeMo-cofactor and P-cluster pair of the nitrogenase molybdenum-iron (MoFe)-protein from Azotobacter vinelandii have been crystallographically verified at 2.2 angstrom resolution. Significantly, no hexacoordinate sulfur atoms are observed in either type of metal center. Consequently, the six bridged iron atoms in the FeMo-cofactor are trigonally coordinated by nonprotein ligands, although there may be some iron-iron bonding interactions that could provide a fourth coordination interaction for these sites. Two of the cluster sulfurs in the P-cluster pair are very close together (∼2.1 angstroms), indicating that they form a disulfide bond. These findings indicate that a cavity exists in the interior of the FeMo-cofactor that could be involved in substrate binding and suggest that redox reactions at the P-cluster pair may be linked to transitions of two cluster-bound sulfurs between disulfide and sulfide oxidation states.
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Cited by
Iron-sulfur clusters: nature's modular, multipurpose structures
Beinert, H., Holm, R. H., & Münck, E. (1997) · Science · doi:10.1126/science.277.5326.653 · Cited by 1,944
Mechanism of molybdenum removal from the sea and its concentration in black shales: EXAFS evidence
Helz, G. R., Miller, C. V., Charnock, J. M., Mosselmans, J. F. W., Pattrick, R. A. D., Garner, C. D., & Vaughan, D. J. (1996) · Geochimica et Cosmochimica Acta · doi:10.1016/0016-7037(96)00195-0 · Cited by 921
Structure–function relationships of alternative nitrogenases
Eady, R. R. (1996) · Chemical Reviews · doi:10.1021/cr950057h · Cited by 877
Huang, Z.-F., Song, J., Li, K., Tahir, M., Wang, Y.-T., Pan, L., Wang, L., Zhang, X., & Zou, J.-J. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b11986 · Cited by 749
Metadata
- Authors
- Chan, M. K., Kim, J., & Rees, D. C.
- Venue
- Science
- Published
- 1993-05-07
- Volume
- 260
- Issue
- 5109
- Pages
- 792-794
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2051499713
- Cited by
- 444
- References
- 0
- FWCI
- 35.92
- Type
- journal article
- Language
- en
- Open access
- closed
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