| Autor: |
Gurbiel RJ; Department of Chemistry, Northwestern University, Evanston, Illinois 60208., Ohnishi T, Robertson DE, Daldal F, Hoffman BM |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry [Biochemistry] 1991 Dec 10; Vol. 30 (49), pp. 11579-84. |
| DOI: |
10.1021/bi00113a013 |
| Abstrakt: |
Electron nuclear double resonance (ENDOR) experiments were performed on 14N (natural abundance) and 15N-enriched iron-sulfur Rieske protein in the ubiquinol-cytochrome c2 oxidoreductase from Rhodobactor capsulatus. The experiments proved that two distinct nitrogenous ligands, histidines, are undoubtedly ligated to the Rieske [2Fe-2S] center. The calculations of hyperfine tensors give values similar but not identical to those of the Rieske-type cluster in phthalate dioxygenase of Pseudomonas cepacia and suggest a slightly different geometry of the iron-sulfur cluster in the two proteins. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
