Radical damage to proteins studied by EPR spin-trapping techniques

Clément, Jean Louis; Gilbert, Bruce C.; Rockenbauer, Antal; Tordo, Paul

doi:10.1039/b103211a

Cited by 21 publications

(12 citation statements)

References 28 publications

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“…In a related study, we reported the oxidation of DMPO to DMPOX by Ce IV without the detection of DMPO/ ⅐ OH (57). Support for the proposal that this latter reaction involves the initial formation of DMPO/ ⅐ OH is provided by the work of Clément et al (68), who, using the DMPO analog 5-(diethylphosphoryl)-5-methyl-1-pyrroline N-oxide (DEPMPO), observed, together with 5-(diethylphosphoryl)-5-methyl-1-pyrrolidone-2-oxyl, a weak signal from DEPMPO/ ⅐ OH. Given that oxygen radical adducts of DMPO are less stable than those of DEPMPO, we consider it reasonable to suggest that, as in the Ce IV /DMPO system, DMPO/ ⅐ OH is an intermediate in the oxidation of DMPO by cyt c/H 2 O 2 .…”

Section: Traces B and D)supporting

confidence: 50%

Evidence for the Role of a Peroxidase Compound I-type Intermediate in the Oxidation of Glutathione, NADH, Ascorbate, and Dichlorofluorescin by Cytochrome c/H2O2

Lawrence

Jones

Wardman

et al. 2003

Journal of Biological Chemistry

160

106

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The release of cytochrome c from mitochondria is a crucial step in apoptosis, resulting in the activation of the caspase proteases. A further consequence of cytochrome c release is the enhanced mitochondrial production of superoxide radicals (O 2 . ), which are converted to hydrogen peroxide by manganese-superoxide dismutase. Recently, we showed that cytochrome c is a potent catalyst of 2,7-dichlorofluorescin oxidation to the fluorescent 2,7-dichlorofluorescein by these species, leading to the conclusion that 2,7-dichlorofluorescein fluorescence is a reflection of cytosolic cytochrome c concentration rather than "reactive oxygen species" levels (Burkitt, M. J., and Wardman, P.

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Section: Traces B and D)supporting

confidence: 50%

Evidence for the Role of a Peroxidase Compound I-type Intermediate in the Oxidation of Glutathione, NADH, Ascorbate, and Dichlorofluorescin by Cytochrome c/H2O2

Lawrence

Jones

Wardman

et al. 2003

Journal of Biological Chemistry

160

106

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“…[37] Reactions of BSA and Lysozyme with HO · Under Normoxic Conditions Addition of Fe 2þ /EDTA to an aqueous solution of BSA, H 2 O 2 and DEPMPO in normoxic conditions, at 08C led to the immediate detection of a strong and anisotropic EPR signal shown in Fig. 2a and as observed previously [40] at 258C in both anoxic and normoxic conditions. The optimized spectrum simulation shown in Fig.…”

Section: Model Experiments: Characterization Of Depmpo Adducts Of Metsupporting

confidence: 61%

“…2c and d) as the protein's tertiary structure is denatured to the expected random coil with more freedom of motion. [40] Reaction of HO · (from Fe 2þ /EDTA and H 2 O 2 ) with lysozyme in the presence of DEPMPO in normoxic conditions at 08C led to the detection of the anisotropic spectrum shown in Fig. 2e, with simulation shown in Fig.…”

Section: Model Experiments: Characterization Of Depmpo Adducts Of Metmentioning

confidence: 88%

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Observation of Protein-derived (BSA) Oxygen-centered Radicals by EPR Spin-trapping Techniques

Clément

Gilbert

Rockenbauer

et al. 2002

Free Radical Research

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Electron paramagnetic resonance (EPR) spin-trapping experiments, employing the novel spin-trap DEPMPO, provide evidence for the formation of protein-peroxyl radicals from the reaction of bovine serum albumin (BSA) or lysozyme with HO. in the presence of O2. Spin-trapping leads to the detection of anisotropic spectra of partially immobilized protein-peroxyl spin-adducts; positive identification is based on a novel spectrum simulation approach (through which broadened anisotropic spectra are simulated and compared with experiment) and by comparison of results with those obtained when MeO2. is trapped and the adduct frozen in a solid matrix.

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“…Our initial studies made use of chemical oxidation via the powerful protein oxidant K 2 IrCl 6 (iridium, denoted Ir(IV)) 19 . The results (Supplementary Figs 4 and 5; see discussion in Supplementary Section 6) indicate that oxidized iridium, and not its reduced form (controls), decrease HLPT activity in a predictable concentrationand time-dependent manner.…”

mentioning

confidence: 99%

Electronic modulation of biochemical signal generation

et al. 2014

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Microelectronic devices that contain biological components are typically used to interrogate biology rather than control biological function. Patterned assemblies of proteins and cells have, however, been used for in vitro metabolic engineering, where coordinated biochemical pathways allow cell metabolism to be characterized and potentially controlled on a chip. Such devices form part of technologies that attempt to recreate animal and human physiological functions on a chip and could be used to revolutionize drug development. These ambitious goals will, however, require new biofabrication methodologies that help connect microelectronics and biological systems and yield new approaches to device assembly and communication. Here, we report the electrically mediated assembly, interrogation and control of a multi-domain fusion protein that produces a bacterial signalling molecule. The biological system can be electrically tuned using a natural redox molecule, and its biochemical response is shown to provide the signalling cues to drive bacterial population behaviour. We show that the biochemical output of the system correlates with the electrical input charge, which suggests that electrical inputs could be used to control complex on-chip biological processes.

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Radical damage to proteins studied by EPR spin-trapping techniques

Cited by 21 publications

References 28 publications

Evidence for the Role of a Peroxidase Compound I-type Intermediate in the Oxidation of Glutathione, NADH, Ascorbate, and Dichlorofluorescin by Cytochrome c/H2O2

Evidence for the Role of a Peroxidase Compound I-type Intermediate in the Oxidation of Glutathione, NADH, Ascorbate, and Dichlorofluorescin by Cytochrome c/H2O2

Observation of Protein-derived (BSA) Oxygen-centered Radicals by EPR Spin-trapping Techniques

Electronic modulation of biochemical signal generation

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