Article
Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis.
Biochemistry - 12 Mar 1991
Miller S M, Massey V, Williams C H, Ballou D P, Walsh C T
Abstract excerpt
Mercuric reductase, a flavoprotein disulfide oxidoreductase, catalyzes the two-electron reduction of Hg(II) to Hg(0) by NADPH. As with all the members of this class of proteins, the enzyme is a dimer of identical subunits with two active sites per dimer, each composed of one FAD and catalytically essential residues from both subunits. In the enzyme from Tn501, these residues include, at a minimum, FAD and...
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