Chenas N K, Martsinkiavichene I A, Kulis Iu Iu, Usanov S A
Biokhimiia. 1987 Apr;52(4):643-9.
The reactions of NADPH oxidation by quinones and inorganic complexes catalyzed by NADPH: adrenodoxin reductase were studied. The catalytic constant for the enzyme at pH 7.0 is 20-25 s-1; the oxidative constants for the quinones vary from 5 X 10(5) to 1.1 X 10(3) M-1 s-1 and show an increase with a rise in the one-electron acceptor reduction potential. The mode of adrenodoxin reductase interaction with oxyquinones differs from that of the enzyme interaction with alkyl-substituted quinones and inorganic complexes. NADPH competitively inhibits electron acceptors, whereas NADP+ is a competitive inhibitor of NADPH and a uncompetitive inhibitor of electron acceptors. (Ki = 25 microM). The depth of FAD incorporation into the enzyme molecule as calculated according to the outer sphere electron transfer theory is 6.1 A.
研究了由NADPH:肾上腺皮质铁氧化还原蛋白还原酶催化的醌类和无机配合物对NADPH的氧化反应。该酶在pH 7.0时的催化常数为20 - 25 s-1;醌类的氧化常数在5×10(5)至1.1×10(3) M-1 s-1之间变化,并随着单电子受体还原电位的升高而增加。肾上腺皮质铁氧化还原蛋白还原酶与氧化醌的相互作用模式不同于该酶与烷基取代醌和无机配合物的相互作用模式。NADPH竞争性抑制电子受体,而NADP+是NADPH的竞争性抑制剂和电子受体的非竞争性抑制剂(Ki = 25 microM)。根据外层电子转移理论计算,FAD嵌入酶分子的深度为6.1 Å。