Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide

被引：221

作者：

Mikami, Yoshinori ^{[1
]}

Shibuya, Norihiro ^{[1
]}

Kimura, Yuka ^{[1
]}

Nagahara, Noriyuki ^{[2
]}

Ogasawara, Yuki ^{[3
]}

Kimura, Hideo ^{[1
]}

机构：

[1] Natl Ctr Neurol & Psychiat, Natl Inst Neurosci, Dept Mol Pharmacol, Kodaira, Tokyo 1878502, Japan

[2] Nippon Med Sch, Dept Environm Med, Bunkyo Ku, Tokyo 1138602, Japan

[3] Meiji Pharmaceut Univ, Dept Hyg Chem, Tokyo 2048588, Japan

来源：

BIOCHEMICAL JOURNAL | 2011年 / 439卷

关键词：

dihydrolipoic acid (DHLA); dithiol; hydrogen sulfide (H(2)S); 3-mercaptopyruvate sulfurtransferase (3MST); thioredoxin; CYSTATHIONINE BETA-SYNTHASE; SITE-DIRECTED MUTAGENESIS; RAT-LIVER MITOCHONDRIA; LIPOIC ACID; MERCAPTOPYRUVATE SULFURTRANSFERASE; SUBCELLULAR-DISTRIBUTION; ESCHERICHIA-COLI; OXIDATIVE STRESS; ACTIVE-SITE; L-CYSTEINE;

D O I：

10.1042/BJ20110841

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

H(2)S (hydrogen sulfide) has recently been recognized as a signalling molecule as well as a cytoprotectant. We recently demonstrated that 3MST (3-mercaptopyruvate sulfurtransferase) produces H(2)S from 3MP (3-mercaptopyruvate). Although a reducing substance is required for an intermediate persulfide at the active site of 3MST to release H(2)S, the substance has not been identified. In the present study we show that Trx (thioredoxin) and DHLA (dihydrolipoic acid) associate with 3MST to release H(2)S. Other reducing substances, such as NADPH, NADH, GSH, cysteine and CoA, did not have any effect on the reaction. We also show that 3MST produces H(2)S from thiosulfate. The present study provides a new insight into a mechanism for the production of H(2)S by 3MST.

引用

页码：479 / 485

页数：7

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