The multiple functions of the thiol-based electron flow pathways of Escherichia coli: Eternal concepts revisited

• Published in: Biochimica et biophysica acta 2008-11, Vol.1780 (11), p.1170-1200
• Main Author: Vlamis-Gardikas, Alexios
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Disulfide; Dsb proteins; Electrons; Escherichia coli - enzymology; Escherichia coli - metabolism; Glutaredoxin; Glutaredoxins - chemistry; Glutaredoxins - metabolism; Glutathione; Molecular Sequence Data; NADP - metabolism; Peroxiredoxin; Sulfhydryl Compounds - metabolism; Thiol; Thioredoxin; Thioredoxins - metabolism
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2008.03.013

Electron flow via thiols is a theme with many variations in all kingdoms of life. The favourable physichochemical properties of the redox active couple of two cysteines placed in the optimised environment of the thioredoxin fold allow for two electron transfers in between top biological reductants and ultimate oxidants. The reduction of ribonucleotide reductases by thioredoxin and thioredoxin reductase of Escherichia coli ( E. coli) was one of the first pathways to be elucidated. Diverse functions such as protein folding in the periplasm, maturation of respiratory enzymes, detoxification of hydrogen peroxide and prevention of oxidative damage may be based on two electron transfers via thiols. A growing field is the relation of thiol reducing pathways and the interaction of E. coli with different organisms. This concept combined with the sequencing of the genomes of different bacteria may allow for the identification of fine differences in the systems employing thiols for electron flow between pathogens and their corresponding mammalian hosts. The emerging possibility is the development of novel antibiotics.