The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Redox-Dependent Structural Changes in the Nitrogenase P-Cluster,
Abstract
The structure of the nitrogenase MoFe-protein from Azotobacter vinelandii has been refined to 2.0 A resolution in two oxidation states. EPR studies on the crystals indicate that the structures correspond to the spectroscopically assigned oxidized (P(OX)/M(OX)) and the native or dithionite-reduced (P(N)/M(N)) forms of the enzyme. Both MoFe-protein structures are essentially identical, with the exception of the P-cluster. The MoFe-protein P-cluster in each state is found to contain eight Fe and seven S atoms. Interconversion between the two redox states involves movement of two Fe atoms and an exchange of protein coordination for ligands supplied by a central S atom. In the oxidized P(OX) state, the cluster is coordinated by the protein through six cysteine ligands, Ser-beta188 O gamma, and the backbone amide of Cys-alpha88. In the native P(N) state, Ser-beta188 O gamma and the amide N of Cys-alpha88 no longer coordinate the cluster due to movement of their coordinated Fe atoms toward the central sulfur. Consequently, this central sulfur adopts a distorted octahedral environment with six surrounding Fe atoms. A previously described model of the P-cluster containing 8Fe-8S likely reflects the inappropriate modeling of a single structure to a mixture of these two P-cluster redox states. These observed redox-mediated structural changes of the P-cluster suggest a role for this cluster in coupling electron transfer and proton transfer in nitrogenase.
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Cites
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Lubitz, W., Ogata, H., Rüdiger, O., & Reijerse, E. (2014) · Chemical Reviews · doi:10.1021/cr4005814 · Cited by 2,060
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Structural basis of biological nitrogen fixation
Rees, D. C., Akif Tezcan, F., Haynes, C. A., Walton, M. Y., Andrade, S., Einsle, O., & Howard, J. B. (2005) · Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences · doi:10.1098/rsta.2004.1539 · Cited by 1,120
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Metadata
- Authors
- Peters, J. W., Stowell, M. H. B., Soltis, S. M., Finnegan, M. G., Johnson, M. K., & Rees, D. C.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1997-02-01
- Volume
- 36
- Issue
- 6
- Pages
- 1181-1187
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1974086171
- Cited by
- 481
- References
- 11
- FWCI
- 33.72
- Type
- journal article
- Language
- en
- Open access
- closed
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