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一株假单胞菌中可溶性苯氧化系统的纯化及某些性质

Purification and some properties of a soluble benzene-oxidizing system from a strain of Pseudomonas.

作者信息

Axcell B C, Geary P J

出版信息

Biochem J. 1975 Jan;146(1):173-83. doi: 10.1042/bj1460173.

DOI:10.1042/bj1460173
PMID:167712
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1165286/
Abstract
  1. A soluble enzyme system which oxidizes benzene to cis-1,2-dihydroxycyclohexa-3,5-diene (cis-benzene glycol) was obtained from a species of Pseudomonas grown on benzene as the major carbon source. 2. The system was shown to consist of three protein components. Two of these were non-haem-iron proteins of molecular weight approx. 21,000 and approx. 186,000 and the other was a flavoprotein of molecular weight approx. 60,000. 3. Fe2+ and NADH were essential cofactors for benzene oxidation.
摘要
  1. 从以苯作为主要碳源生长的一种假单胞菌中获得了一种可将苯氧化为顺式-1,2-二羟基环己-3,5-二烯（顺式苯二醇）的可溶性酶系统。2. 该系统由三种蛋白质成分组成。其中两种是分子量约为21,000和约186,000的非血红素铁蛋白，另一种是分子量约为60,000的黄素蛋白。3. Fe2+和NADH是苯氧化的必需辅助因子。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd8d/1165286/02fe62b8c559/biochemj00564-0184-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd8d/1165286/02fe62b8c559/biochemj00564-0184-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd8d/1165286/02fe62b8c559/biochemj00564-0184-a.jpg

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