Results 181 to 190 of about 33,744 (220)
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The Catalytic Mechanism of Peroxiredoxins
2007Peroxiredoxins carry out the efficient reduction of a typically broad range of peroxide substrates through an absolutely conserved, activated cysteine residue within a highly conserved active site pocket structure. Though details of reductive recycling after cysteine sulfenic acid formation at the active site vary among members of different Prx classes,
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Enhanced hyperoxidation of peroxiredoxin 2 and peroxiredoxin 3 in the presence of bicarbonate/CO2
Free Radical Biology and Medicine, 2019Hydrogen peroxide undergoes an equilibrium reaction with bicarbonate/CO2 to produce peroxymonocarbonate (HCO4-). Peroxymonocarbonate is more reactive with thiols than H2O2 but it makes up only a small fraction of the H2O2 in physiological bicarbonate buffers so the increase in rate of oxidation of low molecular weight thiols is modest.
Alexander V, Peskin +2 more
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Peroxiredoxins as biomarkers of oxidative stress
Biochimica et Biophysica Acta (BBA) - General Subjects, 2014Peroxiredoxins (Prxs) are a class of abundant thiol peroxidases that degrade hydroperoxides to water. Prxs are sensitive to oxidation, and it is hypothesized that they also act as redox sensors. The accumulation of oxidized Prxs may indicate disruption of cellular redox homeostasis.This review discusses the biochemical properties of the Prxs that make ...
Rebecca A, Poynton, Mark B, Hampton
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Peroxiredoxin Systems in Mycobacteria
2007Like other actinomycetes Mycobacterium tuberculosis lacks glutathione and, consequently, the glutathione peroxidases that dominate the antioxidant defence of its mammalian hosts. The hydrogen peroxide metabolism of the pathogen has for long been recognised to depend on a heme-containing catalase/peroxidase.
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Peroxiredoxins in Gametogenesis and Embryo Development
2007Reactive oxygen species have been implicated in gametogenesis and embryo development in animals. As peroxiredoxins are now recognized as important protective antioxidant enzymes as well as modulators of hydrogen peroxide-mediated signaling, we addressed here the putative role of this novel family of peroxidases in gamete maturation and during ...
Isabelle, Donnay, Bernard, Knoops
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Sub-cellular biochemistry, 2008
Mitochondria are the major intracellular sites of oxygen consumption producing reactive oxygen species (ROS) as toxic by-products of oxidative phosphorylation, primarily via electron leakage from the respiratory chain. The resultant types of chemical damage to lipids, DNA and proteins are described as well as the broader implications for the ...
Zhenbo, Cao +2 more
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Mitochondria are the major intracellular sites of oxygen consumption producing reactive oxygen species (ROS) as toxic by-products of oxidative phosphorylation, primarily via electron leakage from the respiratory chain. The resultant types of chemical damage to lipids, DNA and proteins are described as well as the broader implications for the ...
Zhenbo, Cao +2 more
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Evolution of the peroxiredoxins.
Sub-cellular biochemistry, 2008Peroxiredoxins compose a superfamily of peroxidases ubiquitously found throughout evolution in prokaryotes, archaea and eukaryotes. These enzymes contain a conserved catalytic peroxidatic cysteine (Cp) in the N-terminal region of the protein. The residues surrounding Cp and the catalytic site appear also to be well conserved.
Bernard, Knoops +2 more
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The peroxiredoxin gene family in
Free Radical Biology and Medicine, 2001Svetlana N Radyuk +2 more
exaly