Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobin

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 abo...

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Published inF1000 research Vol. 4; p. 87
Main Authors Beckerson, Penny, Svistunenko, Dimitri, Reeder, Brandon
Format Journal Article
LanguageEnglish
Published England F1000Research 07.04.2015
F1000 Research Ltd
Subjects
Biomacromolecule-Ligand Interactions
Protein Chemistry & Proteomics
ferryl
peroxide
distal histidine
monomer
peroxidase
Cytoglobin
hexacoordinate
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Summary: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 of wildtype cytoglobin is unstable, but is able to readily oxidize substrates such as guaiacol. In contrast distal histidine mutants of cytoglobin (H81Y and H81V) show very low peroxidase activity but enhanced radical-induced degradation. Therefore, the weakly bound distal histidine appears to modulate ferryl stability and limit haem degradation. These data are consistent with a role of a peroxidase activity of cytoglobin in cell stress response mechanisms.
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Penny Beckerson and Brandon Reeder planned the experiments. Penny Beckerson performed most of the experiments assisted by Dimitri Svistunenko with the EPR data ( Figure 3 and Figure 7C). Brandon Reeder designed and supervised the project. Penny Beckerson, Dimitri Svistunenko and Brandon Reeder analysed the data and wrote the paper. All authors contributed to the revision of the paper and proofread before submission.
Competing interests: No competing interests were disclosed.
ISSN:2046-1402
2046-1402
DOI:10.12688/f1000research.5971.1