期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:1974
卷号:71
期号:10
页码:3906-3910
DOI:10.1073/pnas.71.10.3906
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:Methylene hydroxylation by cytochrome P-450cam (cytochrome m) can be resolved into four distinct steps: substrate addition, mo [->] mos; reduction, mos [->] mrs; dioxygen addition, mrs [->] mO2rs; followed by a second putidaredoxin (Pseudomonas putida ferredoxin)-mediated reduction and product formation. The isolated ferrous oxy-substrate complex exhibits first-order decay kinetics with the relatively slow rate constant of k [unk] 0.01 sec-1, at 25{degrees
关键词:monooxygenase activity ; protein modification ; iron-sulfur protein-cytochrome complex ; fluorescence ; cytochrome P -450