Lesuisse E, Crichton R R, Labbe P
Laboratoire de Biochimie des Porphyrines, Universite Paris, France.
Biochim Biophys Acta. 1990 Apr 19;1038(2):253-9. doi: 10.1016/0167-4838(90)90213-y.
Several NAD(P)H-dependent ferri-reductase activities were detected in sub-cellular extracts of the yeast Saccharomyces cerevisiae. Some were induced in cells grown under iron-deficient conditions. At least two cytosolic iron-reducing enzymes having different substrate specificities could contribute to iron assimilation in vivo. One enzyme was purified to homogeneity: it is a flavoprotein (FAD) of 40 kDa that uses NADPH as electron donor and Fe(III)-EDTA as artificial electron acceptor. Isolated mitochondria reduced a variety of ferric chelates, probably via an 'external' NADH dehydrogenase, but not the siderophore ferrioxamine B. A plasma membrane-bound ferri-reductase system functioning with NADPH as electron donor and FMN as prosthetic group was purified 100-fold from isolated plasma membranes. This system may be involved in the reductive uptake of iron in vivo.
在酿酒酵母的亚细胞提取物中检测到了几种依赖烟酰胺腺嘌呤二核苷酸磷酸（NAD(P)H）的铁还原酶活性。其中一些在缺铁条件下生长的细胞中被诱导产生。至少有两种具有不同底物特异性的胞质铁还原酶可能在体内铁同化过程中发挥作用。一种酶被纯化至同质：它是一种40 kDa的黄素蛋白（FAD），以NADPH作为电子供体，以Fe(III)-EDTA作为人工电子受体。分离出的线粒体可能通过一种“外部”NADH脱氢酶还原多种铁螯合物，但不能还原铁载体铁胺B。从分离出的质膜中纯化出了一个以NADPH作为电子供体、以黄素单核苷酸（FMN）作为辅基的质膜结合铁还原酶系统，其纯化倍数为100倍。该系统可能参与体内铁的还原吸收。
