The Fe-only nitrogenase from Rhodobacter capsulatus: identification of the cofactor, an unusual, high-nuclearity iron-sulfur cluster, by Fe K-edge EXAFS and 57Fe Mössbauer spectroscopy
| Autor: | Klaus Schneider, Bjr Weiss, A. X. Trautwein, J Groppe, Gerald Henkel, M. Kröckel, E Krahn, Achim Müller, SP Cramer |
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| Rok vydání: | 2001 |
| Předmět: |
FeFe cofactor
Iron-Sulfur Proteins spectroscopy Molybdoferredoxin Iron Iron–sulfur cluster Crystal structure Biochemistry Cofactor Rhodobacter capsulatus Mossbauer Inorganic Chemistry chemistry.chemical_compound Mössbauer spectroscopy Nitrogenase Fe nitrogenase Rhodobacter biology Extended X-ray absorption fine structure Chemistry Spectrum Analysis X-Rays biology.organism_classification Trigonal prismatic molecular geometry Crystallography Zinc biology.protein Ferredoxins extended X-ray absorption fine structure |
| Zdroj: | Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 7(1-2) |
| ISSN: | 0949-8257 |
| Popis: | Samples of the dithionite-reduced FeFe protein (the dinitrogenase component of the Fe-only nitrogenase) from Rhodobacter capsulatus have been investigated by Fe-57 Mossbauer spectroscopy and by Fe and Zn EXAFS as well as XANES spectroscopy. The analyses were performed on the basis of data known for the FeMo cofactor and the P cluster of Mo nitrogenases. The prominent Fourier transform peaks of the Fe K-edge spectrum are assigned to Fe-S and Fe-Fe interactions at distances of 2.29 Angstrom and 2.63 Angstrom, respectively. A significant contribution to the Fe EXAFS must be assigned to an Fe backscatterer shell at 3.68 Angstrom, which is an unprecedented feature of the trigonal prismatic arrangement of iron atoms found in the FeMo cofactor of nitrogenase MoFe protein crystal structures. Additional (FeFe)-Fe-... interactions at 2.92 Angstrom and 4.05 Angstrom clearly indicate that the principal geometry, of the P cluster is also conserved. Mossbauer spectra of Fe-57-enriched FeFe protein preparations were recorded at 77 K (20 mT) and 4.2 K (20 mT, 6.2 T), whereby the 4.2 K high-field spectrum clearly demonstrates that the cofactor of the Fe-only nitrogenase (FeFe cofactor) is diamagnetic in the dithionite-reduced ("as isolated") state. The evaluation of the 77 K spectrum is in agreement with the assumption that this cofactor contains eight Fe atoms. In the literature, several genetic and biochemical lines of evidence are presented pointing to a significant structural similarity of the FeFe, the FeMo and and the FeV cofactors. The data reported here provide the first spectroscopic evidence for a structural homology of the FeFe cofactor to the heterometal-containing cofactors, thus substantiating that the FeFe cofactor is the largest iron-sulfur cluster so far found in nature. |
| Databáze: | OpenAIRE |
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