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Accession number;99A0228215
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| Title;Structural and Functional Roles of Hydrogen Bond to Axial Cysteine in Cytochrome P450cam. |
| Author;
YOSHIOKA SHIRO
(Kyoto Univ., Grad. Sch.)
TAKAHASHI SATOSHI
(Kyoto Univ., Grad. Sch.)
ISHIMORI KOICHIRO
(Kyoto Univ., Grad. Sch.)
MORISHIMA ISAO
(Kyoto Univ., Grad. Sch.)
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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.79-81(1998)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;The sulfer atom of the axial cysteine in P450cam is hydrogen-bonded with three peptide NH groups. To clarify the structural and functional roles of hydrogen bonds in P450cam, we have prepared L358P mutant which lacks a hydrogen bond from leusine 358 and investigated the electronic structure and catalytic activity of the mutant by comparing wild type enzyme. As a result, the mutant showed negative redox potential and enhabced epoxidation activity compared to those of wild type enzyme. Our data suggest that the ferryloxy heme posessing a radical character on the oxygen may be involved in catalytic cycle of P450cam. (author abst.) |
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