Interest in protein disulfide bond formation has recently increased because of the prominent
role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that …

The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the
study of oxidative protein folding. Oxidative protein folding refers to the composite process …

Since its discovery in 1991, the bacterial periplasmic oxidative folding catalyst DsbA has
been the focus of intense research. Early studies addressed why it is so oxidizing and how it …

Biofilms are communities of microbial cells that are encapsulated within a self-produced
polymeric matrix. The matrix is critical to the success of biofilms in diverse habitats; however …

Purpose Deinococcus radiodurans is an extremely radioresistant bacterium characterized
by D10 of 10 kGy, and able to grow luxuriantly under chronic ionizing radiation of 60 Gy/h …

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 …

Aims: DsbA catalyzes disulfide bond formation in secreted and outer membrane proteins in
bacteria. In pathogens, DsbA is a major facilitator of virulence constituting a target for …

The Gram‐positive pathogen C orynebacterium diphtheriae exports through the Sec
apparatus many extracellular proteins that include the key virulence factors diphtheria toxin …

Extracytoplasmic thiol-disulfide oxidoreductases (TDORs) catalyze the oxidation, reduction,
and isomerization of protein disulfide bonds. Although these processes have been …

In many gram-positive Actinobacteria, including Actinomyces oris and Corynebacterium
matruchotii, the conserved thiol-disulfide oxidoreductase MdbA that catalyzes oxidative …