Characterization of Human Cytosolic Thioredoxin Mutants with Increasing Side Chain Volumes at Residue-33

摘要

Thioredoxin (Trx) is a small protein that exists in most living organisms, ranging from bacteria to mammals, and acts as a hydrogen donor for ribonucleotide reductase in Escherichia coli. In higher organisms, Trx functions as a general dithiol-disulfide oxidoreductase that is involved in a variety of biological functions, such as protein disulfide reduction, H2O2 reduction, hydrogen donor for ribonucleotide reductase and methionine sulfoxide reductase, regulation of chloroplast photosynthetic enzymes, and redox regulation of transcription factors. Trx basically catalyses the reduction of disulfides in proteins and becomes oxidized. Trx reductase reduces the oxidized Trx with the help of NADPH.