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1.8.2.6
Molybdenum
molybdenum cofactor exists as low- and high-pH species with g and A(95,97Mo) matrices nearly identical to those of sulfite oxidase. No sulfite-induced reduction to MoV is detected. The outer coordination sphere controls substrate binding in SoxCD, permitting access only to protein-bound sulfur via the C-terminal tail of SoxY
745066
1.8.2.6
Molybdenum
subunit SoxC has a Mo-cofactor containing domain
744213
1.8.2.6
Molybdenum
sulfite oxidase-type molybdenum cofactor in subunit SoxC, residue Arg114 involved in the first oxidation step is in close proximity to the molybdenum atiom
745285
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