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Literature summary for 1.14.15.35 extracted from

  • Harris, D.L.
    Oxidation and electronic state dependence of proton transfer in the enzymatic cycle of cytochrome P450eryF (2002), J. Inorg. Biochem., 91, 568-585.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Saccharopolyspora erythraea Q00441
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Saccharopolyspora erythraea NRRL 2338 Q00441
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the oxidation state dependence originates from differential proton affinities while the electronic state dependence of the reduced oxyferrous heme has its origins in subtle differences in network topologies near the transition state of the initial proton transfer event. Simultaneous diprotonation of the distal oxygen of the reduced oxyferrous heme leads to O-O bond scission, using the combined water network and 6-deoxyerythronolide B substrate protonation agents Saccharopolyspora erythraea ?
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additional information the oxidation state dependence originates from differential proton affinities while the electronic state dependence of the reduced oxyferrous heme has its origins in subtle differences in network topologies near the transition state of the initial proton transfer event. Simultaneous diprotonation of the distal oxygen of the reduced oxyferrous heme leads to O-O bond scission, using the combined water network and 6-deoxyerythronolide B substrate protonation agents Saccharopolyspora erythraea NRRL 2338 ?
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?