Isolation and characterization of flavoredoxin, a new flavoprotein that permits in vitro reconstitution of an electron transfer chain from molecular hydrogen to sulfite reduction in the bacterium Desulfovibrio gigas.
Isolation and characterization of flavoredoxin, a new flavoprotein that permits in vitro reconstitution of an electron transfer chain from molecular hydrogen to sulfite reduction in the bacterium Desulfovibrio gigas.
复制标题
风味蛋白的分离和表征，风味蛋白是一种新的黄素蛋白，可在细菌脱硫弧菌中体外重建从分子氢到亚硫酸盐还原的电子传递链。
DOI：
10.1006/abbi.1993.1253
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发表时间：
1993
影响因子：
3.9
通讯作者：
LeGall,J
中科院分区：
文献类型：
--
作者：
Chen,L;Liu,MY;LeGall,J
从脱硫弧菌中分离到的一种新的含FMN的favoprotein为H2分子中亚硫酸氢盐的还原提供了最大的偶联效率。这种蛋白质，这是不同于flavodoxin和其中的名称flavoredoxin建议，是需要重组的氢化酶和亚硫酸氢盐还原酶之间的电子转移链。Ca 2+结合蛋白在该过程中的Ca 2+存在下作为调节剂起作用。发现的膜结合细胞色素c的分子量为104,000 Da，也活跃在这个电子传递链提供了一个解释的周质和细胞质蛋白之间的活力联系，在这种硫酸盐还原细菌。
A new FMN-containing fiavoprotein isolated fromDesulfovibrio gigasprovided maximum coupling efficiency for the reduction of bisulfite from molecular H2. This protein, which is distinct from flavodoxin and for which the name flavoredoxin is proposed, is required for reconstitution of an electron transfer chain between hydrogenase and bisulfite reductase. A Ca2+-binding protein functions as a modulator in the presence of Ca2+in the process. The finding of a membrane-bound cytochrome c with a molecular weight of 104,000 Da that is also active in this electron transfer chain provides an explanation for the energetic linkage between periplasmic and cytoplasmic proteins in this sulfate-reducing bacterium.