Open AccessCysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis
Author(s) -
Heng Song,
Ampon Sae Her,
Fiona Raso,
Zhi-Bin Zhen,
Yuda Huo,
Pinghua Liu
Publication year - 2014
Publication title -
organic letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.94
H-Index - 239
eISSN - 1523-7060
pISSN - 1523-7052
DOI - 10.1021/ol5005438
Subject(s) - chemistry , cysteine , ergothioneine , histidine , enzyme , biochemistry , heme , biosynthesis , cystine , oxidative phosphorylation , sulfinic acid , catalysis , organic chemistry , antioxidant
OvoA in ovothiol biosynthesis is a mononuclear non-heme iron enzyme catalyzing the oxidative coupling between histidine and cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regio-selectivity. Due to the potential application of this reaction for industrial ergothioneine production, in this study, we systematically characterized OvoA by a combination of three different assays. Our studies revealed that OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. Remarkably, these OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, histidine.