Premium
Substrate specificity of camphor‐induced cytochrome P‐450 Immobilized on an electrode
Author(s) -
Sugihara Nobuhiro,
Ogoma Yoshiro,
Abe Koji,
Murakami Yoshimasa,
Kondo Yoshiyuki,
Akaike Toshihiro
Publication year - 1998
Publication title -
polymers for advanced technologies
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.61
H-Index - 90
eISSN - 1099-1581
pISSN - 1042-7147
DOI - 10.1002/(sici)1099-1581(199812)9:12<858::aid-pat843>3.0.co;2-f
Subject(s) - camphor , substrate (aquarium) , cytochrome , hydroxylation , electrode , cytochrome p450 , electron transfer , materials science , chemistry , biochemistry , enzyme , photochemistry , biology , organic chemistry , ecology
The substrate specificity of a camphor‐induced cytochrome P‐450 (P‐450 cam ) was measured by using a new assay system: electrochemical control of P‐450 cam activity by protein immobilization on an electrode. Immobilized P‐450 cam showed the obvious substrate specificity for hydroxylation of the substrate, suggesting that the simple assay system is applicable for the study of the effect of the other components of the electron transfer system on activity. Copyright © 1998 John Wiley & Sons, Ltd.