Structural and mechanistic aspects of S-S bonds in the thioredoxin-like family of proteins

• Type: Another Publication in an International Scientific Journal
• Date: 2019

Authors

Sergio Filipe Sousa (Author) FCUP; Neves, RPP (Author) FCUP; Waheed, SO (Author) Other; Pedro A Fernandes (Author) FCUP; Ramos, MJ (Author) FCUP

Journal

The Journal is awaiting validation by the Administrative Services.

Title: BIOLOGICAL CHEMISTRY

Vol. 400

Pages: 575-587

ISSN: 1431-6730

Publisher: Walter De Gruyter

Indexing

ISI Web of Knowledge - 14 Citations

Scopus - 16 Citations

Other information

Authenticus ID: P-00P-VKW

DOI: 10.1515/hsz-2018-0319

Abstract (EN): Disulfide bonds play a critical role in a variety of structural and mechanistic processes associated with proteins inside the cells and in the extracellular environment. The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Here, we review the structural and mechanistic determinants behind the thiol-disulfide exchange reactions for the different enzyme types within this family, rationalizing the known experimental data in light of the results from computational studies. The analysis sheds new atomic-level insight into the structural and mechanistic variations that characterize the different enzymes in the family, helping to explain the associated functional diversity. Furthermore, we review here a pattern of stabilization/destabilization of the conserved active-site cysteine residues presented beforehand, which is fully consistent with the observed roles played by the thioredoxin family of enzymes.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 13