Ontology highlight
ABSTRACT:
SUBMITTER: Beckerson P
PROVIDER: S-EPMC4431388 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Beckerson Penny P Svistunenko Dimitri D Reeder Brandon B
F1000Research 20150407
The reaction of hydrogen peroxide with ferric human cytoglobin and a number of distal histidine variants were studied. The peroxidase activity of the monomeric wildtype protein with an internal disulfide bond, likely to be the form of the protein in vivo, exhibits a high peroxidase-like activity above that of other globins such as myoglobin. Furthermore, the peroxidatic activity of wildtype cytoglobin shows increased resistance to radical-based degradation compared to myoglobin. The ferryl form ...[more]