Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis.

doi:10.1021/bi00224a006

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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...

Topics

Binding Sites
Catalysis
Escherichia coli
Kinetics
Mathematics
Mutation
NADP
Oxidation-Reduction
Oxidoreductases
Spectrometry, Fluorescence

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