1.15.1.2	cytochrome c	artificial electron carrier	390148	
1.15.1.2	desulforedoxin	endogenous, contains Zn2+, the protein is able to transfer electrons to superoxide reductase with a maximum kapp of 31/min at an ionic strength of 57 mM, the enzyme complex with superoxide reductase is not detected by chemical shift perturbation	727313	
1.15.1.2	desulforedoxin	from Desufovibrio gigas, recombinantly expressed	726902	
1.15.1.2	additional information	structure of the neelaredoxin center, oxidized and reduced forms, overview	714326	
1.15.1.2	additional information	the active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, that functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction	715670	
1.15.1.2	additional information	the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview	714326	
1.15.1.2	additional information	titration of Zn-rubredoxin with superoxide reductase, overview. NMR competition assay between desulforedoxin and rubredoxin for binding to SOR, overview	727313	
1.15.1.2	reduced rubredoxin	-	674937, 684111, 686522, 686523, 687278, 687582, 687820	
1.15.1.2	reduced rubredoxin	a potential Rd binding site is located in the vicinity of the solvent-exposed residues that are close to the iron centre	686522	
1.15.1.2	reduced rubredoxin	encoded by gene rub	686522	
1.15.1.2	reduced rubredoxin	rubredoxin is reduced by ferredoxin:NADP+ reductase from spinach and NADPH	686751	
1.15.1.2	rubredoxin	-	744022	
1.15.1.2	rubredoxin	assumed to be the phsiological electron carrier	390148	
1.15.1.2	rubredoxin	contains on-heme [Fe(His)4Cys] active sites. Enzymatic reduction of the enzyme iron sites with use of NADH:rubredoxin oxidoreductase and rubredoxin, both from Thermotoga maritima, rates of enzymatic reduction of the ferric center I and enzyme sites are measured	726989	
1.15.1.2	rubredoxin	endogenous rubredoxin, recombinantly expressed	726902	
1.15.1.2	rubredoxin	endogenous. A monomeric, non-heme iron protein that contains a tetrahedral FeS4 metal center. The rubredoxin surface involved in the electron transfer complex with superoxide reductase comprises the solvent-exposed hydrophobic residues in the vicinity of its metal center, Cys9, Gly10, Cys42, Gly43, and Ala44. Kd of 0.003 mM at 59 mM ionic strength by NMR. Model structure of superoxide reductase-rubredoxin complex, overview	727313	
1.15.1.2	rubredoxin	rubredoxins, small proteins with a [FeCys4] center known to be involved in electron transfer processes, are generally assumed to be the direct electron donors to SOR, based on the fact that the genes encoding rubredoxin and SOR lie in the same operon in some bacteria. Consistently, reduced rubredoxins are shown to reduce both 1Fe- and 2Fe-SORs, but physiological electron donors other than rubredoxins must exist because rubredoxins are missing in a large number of organisms that encode SORs	727572