The formation of histidinyl radical (HR), which is a product of electron transfer reaction between histidine and some free radicals, was studied by pulse radiolysis. The reaction between histidine and azide radicals was found to produce HR, which has a distinct absorption spectrum with peaks at 300, 480 and 520 nm. The formation of HR was found to depend solely on the concentration of azide radicals, with the first order rate of 1.46 x 104 s-1. The implication of the formation of HR in an enzyme, which has histidine as the crucial amino acid to its activity, is discussed.Keywords: Histidine, Histidinyl radical, Azide radical
The role of non-coordinated histidines in the iron release mechanism of human serum transferrin has ...
This work is licensed under a Creative Commons Attribution 4.0 International License.Free radical pa...
Electron transfer reduction of gas-phase ions generated from histidine-containing peptides forms sta...
The formation of histidinyl radical (HR), which is a product of electron transfer reaction between ...
The one-electron reduction of chymotrypsin, trypsin, and their zymogens have been studied by pulse r...
International audienceElectron-transfer and -capture dissociations of doubly protonated peptides gav...
Horseradish peroxidase, when incubated with diethyl pyrocarbonate (DEPC), a histidine-specific reage...
Photo oxidation of proteins leads to the formation of cross links of the amino acids in the proteins...
Horseradish peroxidase (HRP), when incubated with diethylpyrocarbonate (DEPC), shows a time-dependen...
A histidine auxotroph of Saccharomyces cerevisiae has been used to metabolically incorporate [1,3-15...
AbstractThe oxidation of proteins by free radicals is thought to play a major role in many oxidative...
AbstractWe report a promising finding that oxidative modification of proteins by free radicals could...
Thymidine radical cation (1) is produced by ionizing radiation and has been invoked as an intermedia...
Agence Nationale de la Recherche, Grant/Award Numbers: ANR-10-LABX-0066 and ANR-11-IDEX-0007; Austri...
Free radicals are species with unpaired electron in their outermost shell. Most free radicals come f...
The role of non-coordinated histidines in the iron release mechanism of human serum transferrin has ...
This work is licensed under a Creative Commons Attribution 4.0 International License.Free radical pa...
Electron transfer reduction of gas-phase ions generated from histidine-containing peptides forms sta...
The formation of histidinyl radical (HR), which is a product of electron transfer reaction between ...
The one-electron reduction of chymotrypsin, trypsin, and their zymogens have been studied by pulse r...
International audienceElectron-transfer and -capture dissociations of doubly protonated peptides gav...
Horseradish peroxidase, when incubated with diethyl pyrocarbonate (DEPC), a histidine-specific reage...
Photo oxidation of proteins leads to the formation of cross links of the amino acids in the proteins...
Horseradish peroxidase (HRP), when incubated with diethylpyrocarbonate (DEPC), shows a time-dependen...
A histidine auxotroph of Saccharomyces cerevisiae has been used to metabolically incorporate [1,3-15...
AbstractThe oxidation of proteins by free radicals is thought to play a major role in many oxidative...
AbstractWe report a promising finding that oxidative modification of proteins by free radicals could...
Thymidine radical cation (1) is produced by ionizing radiation and has been invoked as an intermedia...
Agence Nationale de la Recherche, Grant/Award Numbers: ANR-10-LABX-0066 and ANR-11-IDEX-0007; Austri...
Free radicals are species with unpaired electron in their outermost shell. Most free radicals come f...
The role of non-coordinated histidines in the iron release mechanism of human serum transferrin has ...
This work is licensed under a Creative Commons Attribution 4.0 International License.Free radical pa...
Electron transfer reduction of gas-phase ions generated from histidine-containing peptides forms sta...