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

Reeder, B and Beckerson, P and Svistunenko, D (2015) 'Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobin.' F1000Research, 4. ISSN 2046-1402

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Abstract

© 2015 Beckerson P et al. 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.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 03 Jul 2015 07:28
Last Modified: 15 Oct 2019 11:15
URI: http://repository.essex.ac.uk/id/eprint/14223

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