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- W1968532376 abstract "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." @default.
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- W1968532376 date "1991-10-01" @default.
- W1968532376 modified "2023-10-14" @default.
- W1968532376 title "Enhanced axial symmetry at the Fe3+-heme center of peroxidase by ascorbate: A basis for the ascorbate-dependent peroxidase action" @default.
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- W1968532376 doi "https://doi.org/10.1016/s0006-291x(05)81107-6" @default.
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