Oxidative damage can have a devastating effect on the structure and activity of proteins, and
may even lead to cell death. The sulfur-containing amino acids cysteine and methionine are …

Reactive oxygen species (ROS) are generated as by-products of cellular metabolism,
primarily in the mitochondria. When cellular production of ROS overwhelms its antioxidant …

Extensively revised, the fourth edition of this highly successful book takes into account the
many newly determined protein structures that provide molecular insight into chemiosmotic …

The endoplasmic reticulum (ER) provides an environment that is highly optimized for
oxidative protein folding. Rather than relying on small molecule oxidants like glutathione, it …

Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and
the periplasmic space of prokaryotic cells. The main pathways that catalyse the formation of …

Two-component signal-transducing systems are ubiquitously distributed communication
interfaces in bacteria. They consist of a histidine kinase that senses a specific environmental …

It is generally believed that diseases caused by oxidative stress should be treated with
antioxidants. However, clinical trials with such antioxidants as ascorbic acid and vitamin E …

Cytochrome bd is a respiratory quinol: O2 oxidoreductase found in many prokaryotes,
including a number of pathogens. The main bioenergetic function of the enzyme is the …

The ER-mitochondrial interface is central to calcium signaling, organellar dynamics, and
lipid biosynthesis. The ER and mitochondrial membranes also host sources and targets of …

Cysteine thiols are among the most reactive functional groups in proteins, and their pairing
in disulfide linkages is a common post-translational modification in proteins entering the …