Abstract
Reconstitution of native and ruthenium-modified sperm whale myoglobins (Mb and Ru3Mb) with [OsII(MIX)(CO)(EtOH)] (MIX = mesoporphyrin IX-dicarboxylic acid) and [OsII(MIX)(DMF)2] yields carbonyl osmoglobin ([OsII(CO)][Mb]) and oxidized osmoglobins ([OsIII][Mb], [OsIII][Ru3Mb]). The visible spectrum of [OsII(CO)][Mb] exhibits α and β bands at 538 and 510 nm, respectively. The ascorbate reduction of dioxygen to water is catalyzed by [OsIII][Ru3Mb].
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Contribution No. 7720 from the Arthur Amos Noyes Laboratory, California Institute of Technology, Pasadena, California 911255, U.S.A., and the Department of Chemistry, University of Hong Kong, Pokfulam Road, Hong Kong.
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Che, CM., Chiang, HJ., Margalit, R. et al. Preparation and properties of osmoglobins. Oxidation-reduction catalytic activity of ruthenated osmoglobin. Catal Lett 1, 51–54 (1988). https://doi.org/10.1007/BF00765353
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DOI: https://doi.org/10.1007/BF00765353