The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases.

Amir Porat, Seung-Hyun Cho, Jon Beckwith

Journal: Research in microbiology 2005;155(8):617-22

PMID: 15380548

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Abstract

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.

Address: Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.

DOI: 10.1016/j.resmic.2004.05.005

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MeSH Terms: Cell Membrane, Disulfides, Electron Transport, Escherichia coli, NADH, NADPH Oxidoreductases, Protein Disulfide-Isomerases