IRON-REDUCTASES IN THE YEAST SACCHAROMYCES-CEREVISIAE
IRON-REDUCTASES IN THE YEAST SACCHAROMYCES-CEREVISIAE
复制标题
DOI：
10.1016/0167-4838(90)90213-y
复制
发表时间：
1990-04-19
期刊：
影响因子：
--
通讯作者：
LABBE, P
中科院分区：
文献类型：
--
作者：
LESUISSE, E;CRICHTON, RR;LABBE, P
在酿酒酵母亚细胞提取物中检测到几种依赖NAD(P) h的铁还原酶活性。有些是在缺铁条件下生长的细胞中诱导的。至少有两种具有不同底物特异性的胞质铁还原酶可以促进体内铁的同化。其中一种酶被纯化到均匀性：它是一种40 kDa的黄素蛋白（FAD），以NADPH为电子供体，Fe(III)-EDTA为人工电子受体。分离的线粒体可能通过“外部”NADH脱氢酶还原了多种铁螯合物，但不是铁载体铁胺b。一个以NADPH为电子供体，FMN为假基的质膜结合铁还原酶系统从分离的质膜中纯化了100倍。该系统可能参与体内铁的还原吸收。
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.