Low-molecular-weight oxidants involved in disulfide bond formation.
CONCLUSIONS
The biogenesis of most secreted and outer membrane proteins involves the formation of structure stabilizing disulfide bonds. Hence knowledge of the mechanisms for their formation is critical for understanding a myriad of cellular processes and associated disease states.


BACKGROUND
Until recently it was thought that members of the Ero1 sulfhydryl oxidase family were responsible for catalyzing the majority of disulfide bond formation in the endoplasmic reticulum. However, multiple eukaryotic organisms are now known to show no or minor phenotypes when these enzymatic pathways are disrupted, suggesting that other pathways can catalyze disulfide bond formation to an extent sufficient to maintain normal physiology.


CONCLUSIONS
This lack of a strong phenotype raises multiple questions regarding what pathways are acting and whether they themselves constitute the major route for disulfide bond formation. This review critically examines the potential low molecular oxidants that maybe involved in the catalyzed or noncatalyzed formation of disulfide bonds, with an emphasis on the mammalian endoplasmic reticulum, via an examination of their thermodynamics, kinetics, and availability and gives pointers to help guide future experimental work.
Department of Biochemistry, University of Oulu, Finland. lloyd.ruddock@oulu.fi
Lloyd W
LW
Ruddock
D001205:Ascorbic Acid / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D008970:Molecular Weight; D016877:Oxidants / Q000737:chemistry / Q000378:metabolism*; D010101:Oxygen Consumption; D017382:Reactive Oxygen Species / Q000378:metabolism; D014812:Vitamin K / Q000378:metabolism
D004220:Disulfides; D016877:Oxidants; D017382:Reactive Oxygen Species; D014812:Vitamin K; D006861:Hydrogen Peroxide; D005978:Glutathione; D001205:Ascorbic Acid