The iron-sulfur environment in rubredoxin.
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.
D000042:Absorption; D055598:Chemical Phenomena; D002621:Chemistry; D002627:Chemistry, Physical; D003013:Clostridium; D005288:Ferredoxins; D007501:Iron; D010084:Oxidation-Reduction; D011789:Quantum Theory; D012416:Rubredoxins; D013455:Sulfur; D013696:Temperature; D013816:Thermodynamics; D014965:X-Rays
D005288:Ferredoxins; D012416:Rubredoxins; D013455:Sulfur; D007501:Iron