Organisms employ one of several different enzyme systems to mature cytochromes c. The
biosynthetic process involves the periplasmic reduction of cysteine residues in the heme c …

Almost all organisms, from bacteria to humans, possess catalytic systems that promote
disulfide bond formation‐coupled protein folding, ie oxidative protein folding. These systems …

The respiratory pathogen Streptococcus pneumoniae has evolved efficient mechanisms to
resist oxidative stress conditions and to displace other bacteria in the nasopharynx. Here we …

The biosynthesis of Fe–S clusters and other thio-cofactors requires the participation of redox
agents. A shared feature in these pathways is the formation of transient protein persulfides …

BdbD is a thiol: disulfide oxidoreductase (TDOR) from Bacillus subtilis that functions to
introduce disulfide bonds in substrate proteins/peptides on the outside of the cytoplasmic …

In the actinobacterium Streptomyces lividans copper homeostasis is controlled through the
action of the metalloregulator CsoR. Under copper stress, cuprous ions bind to apo-CsoR …

FipB, an essential virulence factor of Francisella tularensis, is a lipoprotein with two
conserved domains that have similarity to disulfide bond formation A (DsbA) proteins and …

The bacterial endospore is a dormant and heat‐resistant form of life. StoA (SpoIVH) in
Bacillus subtilis is a membrane‐bound thioredoxin‐like protein involved in endospore cortex …

Rhodanese homology domains (RHDs) play important roles in sulfur trafficking mechanisms
essential to the biosynthesis of sulfur-containing cofactors and nucleosides. We have now …

The acidity of small alkylthiols depends mainly on the inductive effect of substituents, and the
ionization state of neighbor functional groups. Protein thiols have a wide range of pK as …