Thiol chemistry in peroxidase catalysis and redox signaling.
The oxidation chemistry of thiols and disulfides of biologic relevance is described. The review focuses on the interaction and kinetics of hydrogen peroxide with low-molecular-weight thiols and protein thiols and, in particular, on sulfenic acid groups, which are recognized as key intermediates in several thiol oxidation processes. In particular, sulfenic and selenenic acids are formed during the catalytic cycle of peroxiredoxins and glutathione peroxidases, respectively. In turn, these enzymes are in close redox communication with the thioredoxin and glutathione systems, which are the major controllers of the thiol redox state. Oxidants formed in the cell originate from several different sources, but the major producers are NADPH oxidases and mitochondria. However, a different role of the oxygen species produced by these sources is apparent as oxidants derived from NADPH oxidase are involved mainly in signaling processes, whereas those produced by mitochondria induce cell death in pathways including also the thioredoxin system, presently considered an important target for cancer chemotherapy.
Bindoli
Alberto
A
Institute of Neurosciences (CNR) c/o Department of Biological Chemistry, University of Padova (Italy). alberto.bindoli@bio.unipd.it
Fukuto
Jon M
JM
Forman
Henry Jay
HJ
D002384:Catalysis; D006861:Hydrogen Peroxide / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D015398:Signal Transduction; D013438:Sulfhydryl Compounds / Q000737:chemistry / Q000378:metabolism*
D013438:Sulfhydryl Compounds; D006861:Hydrogen Peroxide; D010544:Peroxidases