[硝基酪氨酸]细胞色素c。铁结合、蛋白质变性剂及氧化还原电位的影响研究
[Nitrotyrosyl]cytochrome c. Studies of the effect of iron binding, protein denaturants and oxidation-reduction potentials.
作者信息
Do Nascimento A J
出版信息
Biochem J. 1976 Jun 1;155(3):589-97. doi: 10.1042/bj1550589.
Static measurements of the reaction of ligand binding were done by conventional spectrophotometry. The ligand-binding reactions with nitrated cytochrome c were performed with imidazole, iminazole, CO and NO. The stoicheiometry was found to be 1:1, and the stability constants for the complexes formed between the nitrated cytochrome c and the ligands are: 2.58 X 10(4) M-1 (imidazole); 1.01 X 10(2) M-1 (iminazole); 3.6 X 10(4) M-1 (CO); 2.74 X 10(4) M-1 (NO). It was found that the electrometric potentials at pH 7.0 and 25degreesC of [aminotyrosyl]cytochrome c are E'o form II = 0.115 V and E'o form I = 0.260 V, where forms I and II are two species of protein co-existing in the protein solution. The isoelectric point for the oxidized form of [nitrotyrosyl]cytochrome c was 10.05, at 4degreesC.
通过传统分光光度法对配体结合反应进行静态测量。用咪唑、亚氨基咪唑、一氧化碳和一氧化氮进行与硝化细胞色素c的配体结合反应。发现化学计量比为1:1，硝化细胞色素c与配体形成的配合物的稳定常数为：2.58×10⁴ M⁻¹（咪唑）；1.01×10² M⁻¹（亚氨基咪唑）；3.6×10⁴ M⁻¹（一氧化碳）；2.74×10⁴ M⁻¹（一氧化氮）。发现在pH 7.0和25℃下，[氨基酪氨酰基]细胞色素c的电动势为E'o形式II = 0.115 V，E'o形式I = 0.260 V，其中形式I和形式II是在蛋白质溶液中共存的两种蛋白质。在4℃时，[硝基酪氨酰基]细胞色素c氧化形式的等电点为10.05。
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