The disulfide bond formation (Dsb) system

Koreaki Ito, Kenji Inaba

Research output: Contribution to journalReview articlepeer-review

125 Citations (Scopus)


In oxidative folding of proteins in the bacterial periplasmic space, disulfide bonds are introduced by the oxidation system and isomerized by the reduction system. These systems utilize the oxidizing and the reducing equivalents of quinone and NADPH, respectively, that are transmitted across the cytoplasmic membrane through integral membrane components DsbB and DsbD. In both pathways, alternating interactions between a Cys-XX-Cys-containing thioredoxin domain and other regulatory domain lead to the maintenance of oxidized and reduced states of the specific terminal enzymes, DsbA that oxidizes target cysteines and DsbC that reduces an incorrect disulfide to allow its isomerization into the physiological one. Molecular details of these remarkable biochemical cascades are being rapidly unraveled by genetic, biochemical, and structural analyses in recent years.

Original languageEnglish
Pages (from-to)450-458
Number of pages9
JournalCurrent Opinion in Structural Biology
Issue number4
Publication statusPublished - 2008 Aug


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