Agostinho M, Oliveira S, Broco M, Liu M Y, LeGall J, Rodrigues-Pousada C
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Biochem Biophys Res Commun. 2000 Jun 16;272(3):653-6. doi: 10.1006/bbrc.2000.2834.
Sulfate-reducing bacteria are rich in unique redox proteins and electron carriers that participate in a variety of essential pathways. Several studies have been carried out to characterize these proteins, but the structure and function of many are poorly understood. Many Desulfovibrio species can grow using hydrogen as the sole energy source, indicating that the oxidation of hydrogen with sulfite as the terminal electron acceptor is an energy-conserving mechanism. Flavoredoxin is an FMN-binding protein isolated from the sulfate-reducing bacteria Desulfovibrio gigas that participates in the reduction of bisulfite from hydrogen. Here we report the cloning and sequencing of the flavoredoxin gene. The derived amino acid sequence exhibits similarity to several flavoproteins which are members of a new family of flavin reductases suggested to bind FMN in a novel mode.
硫酸盐还原菌富含独特的氧化还原蛋白和电子载体,这些物质参与多种重要途径。已经开展了多项研究来表征这些蛋白质,但许多蛋白质的结构和功能仍知之甚少。许多脱硫弧菌属物种能够以氢气作为唯一能源生长,这表明以亚硫酸盐作为末端电子受体的氢气氧化是一种能量守恒机制。风味氧化还原蛋白是一种从硫酸盐还原菌巨大脱硫弧菌中分离出的FMN结合蛋白,它参与了由氢气还原亚硫酸氢盐的过程。在此,我们报告风味氧化还原蛋白基因的克隆和测序。推导的氨基酸序列与几种黄素蛋白具有相似性,这些黄素蛋白是一个新的黄素还原酶家族的成员,该家族被认为以一种新的模式结合FMN。