A mechanistic investigation of the C-terminal redox motif of thioredoxin reductase from Plasmodium falciparum.
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ABSTRACT:
SUBMITTER: Snider GW
PROVIDER: S-EPMC3957191 | biostudies-literature | 2014 Jan
REPOSITORIES: biostudies-literature
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A mechanistic investigation of the C-terminal redox motif of thioredoxin reductase from Plasmodium falciparum.
Snider Gregg W GW Dustin Christopher M CM Ruggles Erik L EL Hondal Robert J RJ
Biochemistry 20140117 3
High-molecular mass thioredoxin reductases (TRs) are pyridine nucleotide disulfide oxidoreductases that catalyze the reduction of the disulfide bond of thioredoxin (Trx). Trx is responsible for reducing multiple protein disulfide targets in the cell. TRs utilize reduced β-nicotinamide adenine dinucleotide phosphate to reduce a bound flavin prosthetic group, which in turn reduces an N-terminal redox center that has the conserved sequence CICVNVGCCT, where CIC is denoted as the interchange thiol w ...[more]
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