Vieira B J, Davis D J
Arch Biochem Biophys. 1986 May 15;247(1):140-6. doi: 10.1016/0003-9861(86)90542-4.
Chemical modification studies have been conducted on spinach ferredoxin to determine the nature of the groups on ferredoxin involved in its interaction with its reaction partners. Modification of a limited number (three or four) carboxyl groups or of the single histidine residue resulted in a decreased ability of ferredoxin to participate in NADP photoreduction but not in cytochrome c photoreduction, suggesting that these groups may be involved in interaction with ferredoxin:NADP reductase but are not involved in interaction with the reducing side of Photosystem I. In contrast, modification of amino groups or the single arginine residue on ferredoxin had little effect on the ability of ferredoxin to participate in NADP photoreduction, suggesting these groups are not involved in the interaction of ferredoxin with either ferredoxin:NADP reductase or the reducing side of Photosystem I. Attempts to modify tyrosine residues on ferredoxin resulted in destruction of the iron-sulfur center of the protein.
人们已对菠菜铁氧化还原蛋白进行了化学修饰研究,以确定铁氧化还原蛋白上参与其与反应伙伴相互作用的基团的性质。对有限数量(三个或四个)的羧基或单个组氨酸残基进行修饰,会导致铁氧化还原蛋白参与NADP光还原的能力下降,但不影响其参与细胞色素c光还原的能力,这表明这些基团可能参与了与铁氧化还原蛋白:NADP还原酶的相互作用,但不参与与光系统I还原侧的相互作用。相反,对铁氧化还原蛋白上的氨基或单个精氨酸残基进行修饰,对铁氧化还原蛋白参与NADP光还原的能力影响很小,这表明这些基团不参与铁氧化还原蛋白与铁氧化还原蛋白:NADP还原酶或光系统I还原侧的相互作用。尝试对铁氧化还原蛋白上的酪氨酸残基进行修饰,导致该蛋白质的铁硫中心遭到破坏。