Fluorometric and spectrophotometric study of heme binding on the apoprotein from a cytochrome b-2-derivative.
Fluorometric and spectrophotometric study of heme binding on the apoprotein from a cytochrome b-2-derivative.
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血红素与细胞色素 b-2 衍生物脱辅基蛋白结合的荧光和分光光度研究。
DOI：
10.1021/bi00858a030
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发表时间：
1967
期刊：
影响因子：
2.9
通讯作者：
Alain Baudras
中科院分区：
文献类型：
--
作者：
Françoise Labeyrie;Ann di Franco;M. Iwatsubo;Alain Baudras
细胞色素 6Z 的衍生物（L-乳酸：细胞色素 c 氧化还原酶，EC 1.1. 2.3）先前已通过酶的胰蛋白酶消化获得；相同酶重结晶后，在上清液中发现类似产物。两者都被称为 noyau cytochromique 62。已经可以从该蛋白质中分离出血红素成分并描述脱辅基蛋白质的一些特性。添加后，hemeis 在中性时与脱辅基蛋白定量结合；重建的血红素蛋白看起来与原始血红素蛋白非常相似；酪氨酸和 ^ N^^ 是上世纪末首次通过光谱观察从血红素和珠蛋白重建血红蛋白，直到最近才获得了 6 型细胞色素的类似数据。这些实验由 Strittmatter (1960) 对来自肝微粒体（摩尔重量 12,700）的细胞色素 65 进行，然后由 Shichi 和 Hackett（1962）对来自绿豆幼苗（摩尔重量 12,000）的细胞色素 6555 和 658i 进行。已知来自面包酵母的细胞色素 62（L-乳酸.-细胞色素 c-氧化还原酶 EC 1.1.2.3.）是一种分子量为 200,000 量级的分子，每 77,000 g 蛋白质含有一个血红素和一个 FMN*1 辅基（Appleby 和 Morton，1954 年；Appleby 等人，1960 年）。正如 Morton (1961) 和 Baudras (1962) 独立表明的那样，这些假体基团之一，黄素，很容易去除；由此产生的脱辅基酶可以被重新
A derivative of cytochrome 6Z (L-lactate: cytochrome c oxidoreductase, EC 1.1. 2.3) has pre-viously been obtained by trypsic digestion of the enzyme; a similar product is found in the supernatant upon recrystallization of the same enzyme. Both are called noyau cytochromique 62. It has been possible to separate the heme constituent from this protein and to describe some of the properties of the apopro-tein. When added, hemeis bound quantitatively to the apoprotein at neutrality; the reconstituted hemoprotein seems quite similar to the original one; tyrosine and^ N^^ ile the first spectroscopically observed recon-stitutions of hemoglobin from hematin and globin date from the end of the last century, only recently similar data have been obtained for 6-type cytochromes. These experiments were performed by Strittmatter (1960) on cytochrome 65 from liver microsomes (mol wt 12,700), then by Shichi and Hackett (1962) for cytochrome 6555 and 658i from mung bean seedlings (mol wt 12,000). It is known that cytochrome 62 from bakers’ yeast (L-lactate.-cytochrome c-oxidoreductase EC 1.1. 2.3.) is a molecule having a molecular weight of order of 200,000 and containing one heme and one FMN* 1 prosthetic group per 77,000 g protein (Appleby and Morton, 1954; Appleby et al., 1960). One of these prosthetic groups, the flavin, is easily removable as was shown independently by Morton (1961) and Baudras (1962); the resulting apoenzyme can be re-