Is novel signal transducer sulfur oxide involved in the redox cycle of persulfide at the catalytic site cysteine in a stable reaction intermediate of mercaptopyruvate sulfurtransferase?

Antioxidants and Redox Signaling

Volumn 16, Issue 8, 2012, Pages 747-753

  Nagahara, Noriyuki ^a   Nirasawa, Takashi ^b   Yoshii, Taro ^c   Niimura, Youichi ^c  

^a NIPPON MEDICAL SCHOOL   (Japan)

^b BRUKER DALTONIK GMBH   (Germany)

^c TOKYO UNIVERSITY OF AGRICULTURE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

3 MERCAPTOPYRUVATE SULFURTRANSFERASE; ANTIOXIDANT; CYSTEINE; HYDROGEN PEROXIDE; SULFIDE; SULFUR OXIDE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHEMICAL REACTION; CONTROLLED STUDY; MASS SPECTROMETRY; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; RAT; SIGNAL TRANSDUCTION;

ANIMALS; CATALYTIC DOMAIN; CYANIDES; CYSTEINE; HYDROGEN PEROXIDE; OXIDANTS; OXIDATION-REDUCTION; OXIDES; RATS; REDUCING AGENTS; SIGNAL TRANSDUCTION; SULFIDES; SULFUR COMPOUNDS; SULFURTRANSFERASES; THIOREDOXINS;

RATTUS;

EID: 84857623740     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2011.4468     Document Type: Article

References (9)

1. Carroll KS, Gao H, Chen H, Stout CD, Leary JA, and Bertozzi CR. A conserved mechanism for sulfonucleotide reduction. PLoS Biol 3: 1418-1435, 2005.
2. Horowitz PM and Bowman S. Oxidative inactivation of rhodanese by hydrogen peroxide produces states that show differential reactivation. J Biol Chem 264: 3311-3316, 1989. (Pubitemid 19063386)
3. Jönsson TJ, Tsang AW, Lowther WT, and Furdui CM. Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin. J Biol Chem 283: 22890-22894, 2008.
4. Nagahara N and Katayama A. Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis. J Biol Chem 280: 34569-23576, 2005.
5. Nagahara N and Nishino T. Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. cDNA cloning, overexpression, and site-directed mutagenesis. J Biol Chem 271: 27395-27401, 1996. (Pubitemid 26367296)
6. Nagahara N, Okazaki T, and Nishino, T. Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis. J Biol Chem 270: 16230-16235, 1995.
7. Nagahara N, Yoshii T, Abe Y, and Matsumura T. Thioredoxindependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation. J Biol Chem 282: 1561-1569, 2007. (Pubitemid 47076697)
8. Shibuya N, Tanaka M, Yoshida M, Ogasawara Y, Togawa T, Ishii K, and Kimura H. 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain. Antioxid Redox Signal 11: 703-714, 2009.
9. Wróbel M. Sulfurtransferase activity and sulfur compound content in Rana temporaria brain following hibernation. Acta Neurobiol Exp 61: 69-72, 2001. (Pubitemid 32187889)