Abstract
The reduction of ferricytochrome c (cyt c III ) complexes and derivatives by two molybdenum(V) cysteine complexes has been investigated as a model for electron transfer in molybdenum enzymes. The reduction of the pyridoxal phosphate (PLP) derivative of cyt c III by di-μ-oxo-bis[oxo(L-cysteinato)molybdenate(V)] (I) proceeds at the same rate and with the same mechanism as the reduction of native cyt c III ; the mononitromonotyrosyl derivative (MNMT) is reduced somewhat faster. The reduction of the cyanide, azide and imidazole complexes of cyt c III by (μ-oxo-bis[oxodihydroxo(L-cysteinato)molybdate(V)] (II) occurs at a greatly reduced rate and with a different mechanism from the reduction of native cyt c III ; the PLP and MNMT derivatives are reduced with similar rates and mechanisms. The reduction of the N-formyl derivative of cyt c III is biphasic for both (I) and (II), with more complicated kinetics. Rate constants for the reactions have been obtained and mechanisms developed.
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