Xun L, Topp E, Orser C S
Department of Bacteriology and Biochemistry, University of Idaho, Moscow 83843.
J Bacteriol. 1992 Sep;174(17):5745-7. doi: 10.1128/jb.174.17.5745-5747.1992.
Pentachlorophenol (PCP) hydroxylase purified from Flavobacterium sp. strain ATCC 39723 converted PCP or 2,3,5,6-tetrachlorophenol to tetrachloro-p-hydroquinone (TeCH) with the co-consumption of O2 and NADPH. The purified enzyme incorporated 18O from 18O2 but not from H218O into the reaction end product TeCH. The results clearly demonstrate that PCP is oxidatively converted to TeCH by a monooxygenase-type enzyme from Flavobacterium sp. strain ATCC 39723.
从黄杆菌属菌株ATCC 39723中纯化得到的五氯苯酚(PCP)羟化酶,在消耗O2和NADPH的同时,将PCP或2,3,5,6 - 四氯苯酚转化为四氯对苯二酚(TeCH)。纯化后的酶将18O2中的18O而非H218O中的18O掺入反应终产物TeCH中。结果清楚地表明,PCP被黄杆菌属菌株ATCC 39723中的一种单加氧酶型酶氧化转化为TeCH。