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Accession number;99A0228203
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| Title;Mechanisms of N-Demethylations and Sulfoxidations by High Valent Intermediates of Heme enzymes. |
| Author;
GOTO YOSHIO
(Graduate Univ. Advances Studies)
WATANABE YOSHIHITO
(Inst. for Molecular Science)
FUKUZUMI SHUN'ICHI
(Osaka Univ., Fac. of Eng.)
DINNOCENZO J P
(Univ. Rochester)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.13th;NO.;PAGE.43-45(1998)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;An oxoferryl porphyrin cation radical has been believed to be active species of N-demethylation or sulfoxidation in the reaction catalyzed by heme enzymes. To elucidate the mechanisms of these reactions, we have examined direct observation of the reaction of oxoferryl porphyrin cation radical of several heme enzymes and a model complex with a series of p-substituted N,N-dimethylanilines or with a series of p-substituted thioanisoles. Relationships between the redox potential of substrate and the kinetic rate constant of the reactions as well as kinetic isotope effects were investigated. The kinetic profiles obtained by the direct observation method we used in this study have clarified the detailed mechanism of those reactions. (author abst.) |
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