Shinagawa E, Matsushita K, Adachi O, Ameyama M
Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University.
J Biochem. 1990 Jun;107(6):863-7. doi: 10.1093/oxfordjournals.jbchem.a123139.
Gluconobacter suboxydans contains membrane-bound D-glucose and alcohol dehydrogenases (GDH and ADH) as the primary dehydrogenases in the respiratory chain. These enzymes are known to be quinoproteins having pyrroloquinoline quinone as the prosthetic group. GDH reduces an artificial electron acceptor, ferricyanide, in the membrane, but not after solubilization with Triton X-100, while ADH can react with the electron acceptor even after solubilization and further purification. In this study, it has been shown that the ferricyanide reductase activity of GDH is restored by adding the supernatant solubilized with Triton X-100 to the residue, and also by incorporation of purified ADH into the membranes of an ADH-deficient strain. G. suboxydans var. alpha. In addition, the ferricyanide reductase activity of GDH was reconstituted in proteoliposomes from GDH, ADH, and ubiquinone-10. Thus, the results indicated that the electron transfer from GDH to ferricyanide was mediated by ubiquinone and ADH. The data also suggest that GDH and ADH transfer electrons mutually via ubiquinone in the respiratory chain.
弱氧化葡糖杆菌含有膜结合的D - 葡萄糖脱氢酶和醇脱氢酶（GDH和ADH），作为呼吸链中的主要脱氢酶。已知这些酶是含有吡咯喹啉醌作为辅基的醌蛋白。GDH可在膜中还原人工电子受体铁氰化物，但在用 Triton X - 100溶解后则不能，而ADH即使在溶解和进一步纯化后仍能与电子受体反应。在本研究中，已表明通过将用Triton X - 100溶解的上清液添加到残渣中，以及将纯化的ADH掺入ADH缺陷菌株的膜中，GDH的铁氰化物还原酶活性得以恢复。弱氧化葡糖杆菌α变种。此外，GDH的铁氰化物还原酶活性在由GDH、ADH和泛醌 - 10组成的蛋白脂质体中得以重建。因此，结果表明从GDH到铁氰化物的电子转移是由泛醌和ADH介导的。数据还表明，GDH和ADH在呼吸链中通过泛醌相互传递电子。
