The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases.
The bacterial membrane protein DsbD transfers electrons across the cytoplasmic membrane to reduce protein disulfide bonds in extracytoplasmic proteins. Its substrates include protein disulfide isomerases and a protein involved in cytochrome c assembly. Two membrane-embedded cysteines in DsbD alternate between the disulfide-bonded (oxidized) and reduced states in this process.
Porat
Amir
A
Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Cho
Seung-Hyun
SH
Beckwith
Jon
J
D002462:Cell Membrane / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry; D004579:Electron Transport; D004926:Escherichia coli / Q000201:enzymology; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry; D019704:Protein Disulfide-Isomerases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D004220:Disulfides; D009247:NADH, NADPH Oxidoreductases; C014703:disulfide reductase (NADH); D019704:Protein Disulfide-Isomerases