Why is DsbA such an oxidizing disulfide catalyst?

U Grauschopf; Jakob R. Winther; P Korber; T Zander; P Dallinger; J C Bardwell

Why is DsbA such an oxidizing disulfide catalyst?

U Grauschopf, Jakob R. Winther, P Korber, T Zander, P Dallinger, J C Bardwell

Biomolecular Sciences

271 Citationer (Scopus)

Abstract

DsbA, a member of the thioredoxin family of disulfide oxidoreductases, acts in catalyzing disulfide bond formation by donating its disulfide to newly translocated proteins. We have found that the two central residues within the active site Cys-30-Pro-31-His-32-Cys-33 motif are critical in determining the exceptional oxidizing power of DsbA. Mutations that change these two residues can alter the equilibrium oxidation potential of DsbA by more than 1000-fold. A quantitative explanation for the very high redox potential of DsbA was found by measuring the pKa of a single residue, Cys-30. The pKa of Cys-30 varied dramatically from mutant to mutant and could accurately predict the oxidizing power of each DsbA mutant protein.

Originalsprog	Engelsk
Tidsskrift	Cell
Vol/bind	83
Udgave nummer	6
Sider (fra-til)	947-55
Antal sider	9
ISSN	0092-8674
Status	Udgivet - 1995

Citationsformater

@article{75434229d9be4178b1537122f326df97,

title = "Why is DsbA such an oxidizing disulfide catalyst?",

abstract = "DsbA, a member of the thioredoxin family of disulfide oxidoreductases, acts in catalyzing disulfide bond formation by donating its disulfide to newly translocated proteins. We have found that the two central residues within the active site Cys-30-Pro-31-His-32-Cys-33 motif are critical in determining the exceptional oxidizing power of DsbA. Mutations that change these two residues can alter the equilibrium oxidation potential of DsbA by more than 1000-fold. A quantitative explanation for the very high redox potential of DsbA was found by measuring the pKa of a single residue, Cys-30. The pKa of Cys-30 varied dramatically from mutant to mutant and could accurately predict the oxidizing power of each DsbA mutant protein.",

keywords = "Amino Acid Sequence, Base Sequence, Binding Sites, Catalysis, Cysteine, Disulfides, Enzyme Stability, Isomerases, Kinetics, Molecular Sequence Data, Mutation, Oxidation-Reduction, Oxidoreductases, Protein Disulfide-Isomerases, Protein Folding, Recombinant Fusion Proteins, beta-Galactosidase",

author = "U Grauschopf and Winther, {Jakob R.} and P Korber and T Zander and P Dallinger and Bardwell, {J C}",

year = "1995",

language = "English",

volume = "83",

pages = "947--55",

journal = "Cell",

issn = "0092-8674",