These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Detection and reactions of the globin radical in haemoglobin.
    Author: McArthur KM, Davies MJ.
    Journal: Biochim Biophys Acta; 1993 Oct 06; 1202(2):173-81. PubMed ID: 8399378.
    Abstract:
    The reaction of methaemoglobin with hydrogen peroxide and other oxidants has been studied using both electron paramagnetic resonance (EPR) and optical spectroscopy. The results obtained are consistent with the formation of an iron(IV)-oxo species (which is one oxidising equivalent above the initial level) and rapid transfer of the second oxidising equivalent into the surrounding globin generating a protein radical; this species has been observed by stopped-flow EPR. The partially resolved hyperfine splittings of the EPR signal (a2H 0.66, a2H 0.17, aH 1.157, aH 0.203 mT), together with its g value (2.0044) suggest that this species is a sterically-constrained tyrosine phenoxyl radical. Experiments with inhibitors and chemically-modified haemoglobins are in agreement with this assignment. This radical is not observed with the apoprotein or oxyhaemoglobin, confirming that the reaction requires the presence of an iron(III) haem. The concentration of the phenoxyl radical is not affected by hydroxyl-radical scavengers but is affected by certain reducing agents and antioxidants, demonstrating that the protein radical is accessible to reagents in bulk solution. Analysis of the protein structure suggests that this radical may be centered on the tyrosine at alpha-42 as this residue is in close proximity to the haem groups and partially exposed on the surface. Addition of the spin trap DMPO to the reaction system results in the observation of a broad, anisotropic, spectrum from a protein-derived spin adduct; this signal is assigned to a peroxyl radical adduct on the basis of the hyperfine coupling constants (aN 2.03, aH 1.4 mT), its short life-time, the detection of oxygen uptake, and the decrease in the intensity of this signal under anoxic conditions. Experiments with modified haemoproteins and inhibitors suggest that this species arises via the tyrosine phenoxyl radical. These observations suggest that the tyrosine residues act as a 'sink' for oxidising equivalents generated by electron-transfer within the protein after initial oxidation at the haem centre.
    [Abstract] [Full Text] [Related] [New Search]