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1 eroxide, a result consistent with it being a superoxide reductase.
2 ixing of the Desulfovibrio vulgaris two-iron superoxide reductase (2Fe-SOR) containing the ferrous ac
5 s FprA lies downstream of an operon encoding superoxide reductase and rubredoxin, consistent with an
10 ces between Fe(II)-M121EAz, Fe(II)-wtAz, and superoxide reductase (SOR) and allowed design of the sec
13 zed and reduced forms of Pyrococcus furiosus superoxide reductase (SOR) as a function of pH and exoge
14 e have added cyanide to oxidized 1Fe and 2Fe superoxide reductase (SOR) as a surrogate for the putati
15 ivo results are presented demonstrating that superoxide reductase (SOR) from the air-sensitive oral s
19 lear iron active site of Pyrococcus furiosus superoxide reductase (SOR) through the use of EPR, reson
20 te kinetics of a Desulfovibrio (D.) vulgaris superoxide reductase (SOR) turnover cycle, in which supe
21 t can act as a superoxide dismutase (SOD), a superoxide reductase (SOR), and a superoxide oxidase (SO
27 s))] structure of the reduced active site of superoxide reductases (SORs), a class of enzymes that de
28 lly to mimic the nonheme iron active site of superoxide reductase, which contains a five-coordinate i
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