Townley H E, Griffiths W T, Nugent J P
Department of Biochemistry, School of Medical Sciences, University of Bristol, UK.
FEBS Lett. 1998 Jan 23;422(1):19-22. doi: 10.1016/s0014-5793(97)01589-5.
It is widely believed that protochlorophyllide reductase is a flavoenzyme effecting catalysis by a radical mechanism. Here the cyanobacterial reductase has been isolated from Escherichia coli overexpressing the Synechocystis gene. The purified enzyme, while retaining full activity, has no detectable flavine. No radical derived ESR signal was observed during catalysis or on photoexcitation under non-catalytic conditions. Mechanistic implications of the findings are discussed.
人们普遍认为原叶绿素酸酯还原酶是一种通过自由基机制进行催化的黄素酶。在这里，蓝藻还原酶是从过量表达集胞藻基因的大肠杆菌中分离出来的。纯化后的酶虽然保留了全部活性，但未检测到黄素。在催化过程中或非催化条件下光激发时，均未观察到自由基衍生的电子顺磁共振信号。本文讨论了这些发现的机制意义。
