重组人细胞质和线粒体NADPH:硫氧还蛋白还原酶氧化还原特性的比较研究

IF 0.5 4区化学 Q4 CHEMISTRY, MULTIDISCIPLINARY

Chemija Pub Date : 2022-05-04 DOI:10.6001/chemija.v33i2.4707

Lina Misevičienė, K. Krikštopaitis, N. Čėnas

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引用次数: 0

摘要

我们比较了重组人黄磺基硒酶NADPH:硫氧还蛋白还原酶的细胞质(TrxR1)和线粒体(TrxR2)异构体的氧化还原特性。根据NADP+/NADPH对氧化还原平衡测定的同工酶(e07)的标准氧化还原电位分别为-0.295 V (TrxR1)和-0.270 V (TrxR2)。TrxR2的e07较高的正值可能是由于His-125存在于催化二硫化物和硒基硫化物附近，而不是TrxR1中的tyrl -116。几种醌类和硝基芳香化合物对TrxR1和TrxR2的反应活性随着其单电子还原电位的增加而增加(E1 7)。我们首次研究了TrxR1催化的一系列芳香n -氧化物的单电子和双电子混合还原。它们的反应活性接近醌类和硝基芳烃类，E1 - 7值相近。

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The comparative study of redox properties of recombinant human cytosolic and mitochondrial NADPH: thioredoxin reductases

We compared the redox properties of recombinant cytosolic (TrxR1) and mitochondrial (TrxR2) isoforms of human flavosulfoselenoenzyme NADPH:thioredoxin reductase. The standard redox potentials of isoenzymes (E0 7), determined according to the redox equilibrium with the NADP+/NADPH couple, were equal to –0.295 V (TrxR1) and –0.270 V (TrxR2). The more positive value of E0 7 of TrxR2 may be attributed to the presence of His-125 at the vicinity of catalytic disulfide and selenylsulfide, instead of Tyr-116 in TrxR1. The reactivity of several quinones and nitroaromatic compounds towards TrxR1 and TrxR2 increased with their single-electron reduction potential (E1 7). For the first time, we studied the TrxR1-catalysed reduction of a series of aromatic N-oxides which were reduced in a mixed single- and two-electron way. Their reactivity was close to that of quinones and nitroaromatics with the similar values of E1 7.

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来源期刊

Chemija 化学-化学综合

CiteScore

1.30

自引率

16.70%

发文量

审稿时长

>12 weeks

期刊介绍： Chemija publishes original research articles and reviews from all branches of modern chemistry, including physical, inorganic, analytical, organic, polymer chemistry, electrochemistry, and multidisciplinary approaches.