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- W2009404435 abstract "Dihdyropteridine reductase (DHPR) catalyzes reduction of the unstable quinonoid dihydropteridine to the active tetrahydropteridine form through the oxidation of NADH. DHPR deficiency or any blockage in biosynthesis of tetrahydropteridine results in development of phenylketonuria (PKU), a progressive neurological illness which does not respond to dietary treatment. It has been speculated that DHPR or metabolites associated with it may have antioxidative properties. In another study, DHPR has been shown to have NADH-ferric reductase activity. This activity is postulated to have an important role in dietary iron uptake. There is an emerging role, though mechanistically unclear at this point, for BH4 in maintaining nitric oxide synthase (NOS) activity. NOS produces the signaling agent nitric oxide (•NO) from L-arginine. In the light of these emerging roles there is a growing need to completely understand how DHPR works. The mechanism of catalysis in DHPR is not fully understood. Previous studies have suggested the involvement of the thiol group of a cysteine residue in DHPR. Using Raman spectroscopic techniques, the effect of the inhibitors/substrate and/or cofactor on the protonation state of the thiol group is investigated. Raman spectroscopy is particularly effective because of a unique peak at ca. 2500 cm-1 due to the S-H stretch and another one at ca. 900 cm-1 due to the C-S bond. Peak shifts and modulation in intensities are monitored and analyzed in terms of its mechanistic implications." @default.
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- W2009404435 date "2009-02-01" @default.
- W2009404435 modified "2023-10-05" @default.
- W2009404435 title "Probing the role of Cys-78 in dihydropteridine reductase (DHPR) using Raman Spectroscopy" @default.
- W2009404435 doi "https://doi.org/10.1016/j.bpj.2008.12.1556" @default.
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