Bell J M, Colby J, Williams E
North East Biotechnology Centre, Biology Department, Sunderland Polytechnic, U.K.
Biochem J. 1988 Mar 1;250(2):605-12. doi: 10.1042/bj2500605.
CO oxidoreductase was purified to 95% homogeneity from crude mycelial extracts of Streptomyces G26. The purified preparation has a specific activity of 25.7 units/mg, a 13-fold improvement on crude soluble mycelial extracts. The native enzyme (Mr 282,000) is composed of non-identical subunits of Mr 110,000 and 33,000. It is a molybdenum hydroxylase containing 1.6 mol of FAD, 7.3 mol of Fe, 8.3 mol of acid-labile sulphide and 1.3 mol of Mo per mol of enzyme. Purified CO oxidoreductase catalyses the reduction of benzyl viologen, confirming the previously reported ability of this enzyme to interact with low-potential acceptors. Cytochrome c reduction cannot be accounted for entirely by non-enzymic reduction by superoxide radicals. NAD+ and NADP+ are not reduced, nor is clostridial ferredoxin.
一氧化碳氧化还原酶从链霉菌G26的粗菌丝体提取物中纯化至95%的纯度。纯化后的制剂比活性为25.7单位/毫克，比粗可溶性菌丝体提取物提高了13倍。天然酶（Mr 282,000）由分子量为110,000和33,000的不同亚基组成。它是一种含钼羟化酶，每摩尔酶含有1.6摩尔FAD、7.3摩尔铁、8.3摩尔酸不稳定硫化物和1.3摩尔钼。纯化的一氧化碳氧化还原酶催化苄基紫精的还原，证实了该酶与低电位受体相互作用的先前报道的能力。细胞色素c的还原不能完全由超氧自由基的非酶促还原来解释。NAD+和NADP+不被还原，梭菌铁氧化还原蛋白也不被还原。
