Abstract
Ruthenium myoglobins have been prepared by the reconstitution of horse heart apomyoglobin with either ruthenium(II) or ruthenium(III) mesoporphyrin IX (MpIX) derivatives. The ruthenium(II) and -(III) myo globins (RuMb and RuMb+, respectively) contain one ruthenium porphyrin/heme binding site; the species are readily interconverted using dithionite for reduction and bromine for oxidation. RuMb binds carbon monoxide to give the known carbonyl complex. Reversible oxygenation occurs readily with protein-free RuII(MpIX) species in dimethylformamide, but RuMb in phosphate buffer is irreversibly oxidized by dioxygen to give RuMb+ via an outer sphere electron transfer mechanism.
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