Enhanced axial symmetry at the Fe(3+)-heme center of peroxidase by ascorbate: a basis for the ascorbate-dependent peroxidase action.
In the absence of its substrate hydrogen peroxide, peroxidase exhibits perturbations in its Fe(3+)-heme center, when incubated with ascorbic acid. The electron paramagnetic pattern sprang towards a higher g-value side, denoting a sharpening of the rhombic axial symmetry around the heme-center. The interpretation is that the ascorbate dependent peroxidase action starts with the formation of an Fe(3+)-ascorbate charge transfer complex intermediate.
Pradeep Kumar
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School of Life Sciences, D. A. Vishwavidyalaya, Vigyan Bhawan, Indore, India.
Sinha
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Laloraya
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Nivsarkar
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D001205:Ascorbic Acid / Q000378:metabolism* / Q000494:pharmacology; D001560:Benzidines / Q000494:pharmacology; D004578:Electron Spin Resonance Spectroscopy; D006139:Guaiacol / Q000494:pharmacology; D006418:Heme / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000737:chemistry / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D011487:Protein Conformation
D001560:Benzidines; C029876:benzidine; D006418:Heme; D006139:Guaiacol; D007501:Iron; D006735:Horseradish Peroxidase; D001205:Ascorbic Acid