Parham R, Rebeiz C A
Laboratory of Plant Pigment Biochemistry and Photobiology, University of Illinois, Urbana 61801, USA.
Anal Biochem. 1995 Oct 10;231(1):164-9. doi: 10.1006/abio.1995.1516.
[4-Vinyl]Chlorophyllide alpha reductase (4VCR) catalyzes the conversion of 2,4-divinyl chlorophyllide alpha (DV Chlide alpha) to 2-vinyl,4-ethyl chlorophyllide alpha (MV Chlide alpha) via an NAPDH- dependent reaction. MV Childe alpha is the immediate precursor of monovinyl chlorophyll alpha in plants. In etiolated cucumber (Cucumis sativus L.) cotyledons, 4VCR is a plastidic membrane-bound enzyme. Further research on this enzyme required the development of an assay that utilizes DV Childe alpha as an exogenous substrate. Such an assay is now described. It involves conversion of exogenous DV Chlide alpha to MV Chlide alpha at high rates by etioplast membranes of cucumber, corn (Zea mays L.), and barley (Hordum vulgare L.). 4VCR exhibits high activity between 30 and 40C and in the pH range of 6.3 to 7.0. Activity is quasilinear for the first 60 s of incubation.
[4-乙烯基]叶绿素酸酯α还原酶（4VCR）通过依赖于烟酰胺腺嘌呤二核苷酸磷酸（NAPDH）的反应催化2,4-二乙烯基叶绿素酸酯α（DV叶绿素酸酯α）转化为2-乙烯基,4-乙基叶绿素酸酯α（MV叶绿素酸酯α）。MV叶绿素酸酯α是植物中单乙烯基叶绿素α的直接前体。在黄化黄瓜（Cucumis sativus L.）子叶中，4VCR是一种质体膜结合酶。对该酶的进一步研究需要开发一种利用DV叶绿素酸酯α作为外源底物的检测方法。现在介绍这样一种检测方法。它涉及黄瓜、玉米（Zea mays L.）和大麦（Hordum vulgare L.）的黄化质体膜将外源DV叶绿素酸酯α快速转化为MV叶绿素酸酯α。4VCR在30至40℃以及pH值为6.3至7.0的范围内表现出高活性。在孵育的前60秒内活性呈准线性。
