| Literature DB >> 890038 |
Abstract
The atomic environment around the iron site in the nonheme iron sulfur protein rubredoxin was studied by the extended X-ray absorption fine structure (EXAFS) technique. Within experimental error, the Fe-S bonds in oxidized Clostridium pasteurianum rubredoxin are the same as in the analogue anion [Fe(S2-o-xyl)2]-synthesized by Holm. The average Fe-S bond length is 2.267 +/- 0.003A and the root mean square deviation about this average due to structural disorder is 0.032 + 0.013 - 0.032.Entities:
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Year: 1977 PMID: 890038 PMCID: PMC1473326 DOI: 10.1016/S0006-3495(77)85585-9
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033