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• W2089470865 abstract "The use of resonance Raman spectroscopy to investigate the mechanistic role of the proximal ligand to the iron of oxygen-activating heme enzymes is discussed. Data are summarized which support the proposal that the σ- and π-donating ability of the proximal ligand (thiolate sulfur in cytochromes P-450, imidazolate nitrogen in peroxidases, tyrosinate oxygen in catalases) promotes electron flow to the π* orbitals of distal peroxide-level dioxygen and is responsible for labilization of the FeOO system. Although additional factors such as the protein environment and substrate accessibility may modulate the properties of the metal site in these enzymes, the fundamental activity of the metal center is most strongly influenced by the proximal ligand. Understanding the properties of the proximal ligand is therefore essential to a complete description of the mechanism of oxygen activation." @default.
• W2089470865 created "2016-06-24" @default.
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• W2089470865 date "1989-12-01" @default.
• W2089470865 modified "2023-09-24" @default.
• W2089470865 title "Towards a unified concept of oxygen activation by heme enzymes: the role of the proximal ligand" @default.
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• W2089470865 doi "https://doi.org/10.1016/0022-2860(89)80011-0" @default.
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