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- W2028007941 abstract "Disulfide oxidoreductases react with substrates through a mixed disulfide intermediate. A second cysteine from either substrate or enzyme can attack the mixed disulfide bond, resulting in substrate oxidation or enzyme release, respectively. During catalyzed oxidative folding, the enzyme acts as a passive placeholder; remaining in a mixed disulfide with a substrate cysteine until folding brings the cognate cysteine into proximity. Therefore, in order for catalyzed oxidative folding to succeed, the enzyme must release with a rate slower than the folding rate of the substrate. We have developed single molecule AFM techniques to monitor the formation of mixed disulfide complexes between substrate and oxidoreductase, which in turn can be used to measure the rates of catalyzed oxidative folding as well as enzyme release. Previously, our group has used these techniques to study PDI, the primary eukaryotic disulfide oxidant. Here we investigate the bacterial analog of PDI, DsbA. For both enzymes, we found that the rate of catalyzed oxidative folding is comparable to the rate of folding of reduced substrate, while a previously oxidized substrate folds roughly 30 times faster. This result entails that oxidation must occur late in the folding process, thus confirming the passive placeholder mechanism. The fact that both enzymes follow the same mechanism suggests that it might be a general model for disulfide oxidoreductase function across all domains of life. Despite the similar mechanisms and in vivo roles of the two enzymes, we found vastly different rates of spontaneous release. DsbA releases at a rate of about 0.01 s-1, which is roughly tenfold slower than PDI. This exceedingly slow rate of release suggests that the repertoire of prokaryotic proteins that are catalytically oxidized may take longer to fold, on average, than their eukaryotic counterparts." @default.
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- W2028007941 date "2014-01-01" @default.
- W2028007941 modified "2023-09-28" @default.
- W2028007941 title "Placeholder Mechanism of Catalyzed Oxidative Folding is Conserved Across Multiple Domains of Life" @default.
- W2028007941 doi "https://doi.org/10.1016/j.bpj.2013.11.3753" @default.
- W2028007941 hasPublicationYear "2014" @default.
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