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- W2023974344 abstract "We report on the electron spin resonance (ESR) study of the photo-oxidative stress-mediated protein conformation changes in the spin-labelled protein staphylococcal nuclease (SNase). The photo-oxidative stress was brought on by photosensitization of singlet oxygen (1Δg) in the presence of a novel photosensitizer, water-soluble fullerol C60(OH)19(ONa)17, and resulted in partial protein denaturation. This process was monitored via ESR measurements performed for a spin-labelled SNase Thr-62-Cys mutant, with MTSSL spin label (SL) attached to the cysteine 62 residue (SNase T62C-SL). Prior to ESR measurements of the oxidative stress-induced alterations in protein conformations, the efficiency of C60(OH)19(ONa)17 for 1Δg-generation was confirmed by three different techniques: (i) selective reactive scavenging of 1Δg and ESR detection of the resulting paramagnetic product, (ii) 1Δg-mediated photo-oxidative loss of tryptophan and (iii) by measuring the characteristic near-infrared phosphorescence of singlet oxygen at 1270 nm. The observed evolution of the ESR spectra of SNase T62C-SL as a function of exposure to the photo-oxidative stress points to marked changes in protein conformation due to the deleterious action of 1Δg." @default.
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- W2023974344 date "2007-06-25" @default.
- W2023974344 modified "2023-10-16" @default.
- W2023974344 title "Oxidative stress-mediated protein conformation changes: ESR study of spin-labelled staphylococcal nuclease" @default.
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- W2023974344 doi "https://doi.org/10.1088/0953-8984/19/28/285201" @default.
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