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ROLES OF THIOL-REDOX PATHWAYS IN BACTERIA
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Journal Article
ROLES OF THIOL-REDOX PATHWAYS IN BACTERIA
2001
Overview
Disulfide bonds in proteins play various important roles. They are either
formed as structural features to stabilize the protein or are found only
transiently as part of a catalytic or regulatory cycle. In vivo, the formation
and reduction of disulfide bonds is catalyzed by specialized thiol-disulfide
exchanging enzymes that contain an active site with the sequence motif
Cys-X-X-Cys. These proteins have structurally evolved to catalyze predominantly
either oxidative reactions or reductive steps. There is mounting evidence that,
in addition to the thiol redox potential, the spatial distribution within
different cell compartments and the overall redox state of the cell are equally
important. In the cytoplasm, multiple pathways play overlapping roles in the
reduction of disulfide bonds and additionally, the expression of several
components of thiol-redox pathways was shown to respond to the changes in the
cellular thiol-redox equilibrium. In the periplasm, two systems coexist, one
catalyzing thiol oxidation and the other disulfide reduction. Recent results
suggest that two different mechanisms are used to translocate reducing power
from the cytoplasm or to dissipate the electrons after oxidation.
Publisher
Annual Reviews,Annual Reviews, Inc
Subject
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - metabolism
/ Biological and medical sciences
/ Escherichia coli - metabolism
/ Experimental bacterial diseases and models
/ Fundamental and applied biological sciences. Psychology
/ Proteins
/ Sulfhydryl Compounds - chemistry
/ Sulfhydryl Compounds - metabolism
/ Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies
