紫外光诱导氧合型肌红蛋白氧化反应及机理

doi:10.3866/PKU.WHXB201601046

Abstract

Abstract:

Myoglobin (Mb) achieves its biological functions such as oxygen transfer and storage in the dark. In this research, we found that UV light irradiation could promote oxidation of ferroporphyrin, which significantly affected the physiological function of oxymyoglobin (MbO₂). The blue shift of the Soret band and decreased intensities of Q-band reduction peaks at 544 and 580 nm observed in UV-Vis absorption spectra revealed that UV light could promote O₂ dissociation, and consequently MbFe(Ⅱ) was oxidized to MbFe(Ⅲ). The effect sequence of wavelength on the strength of this photo-oxidation was 254 nm > 280 nm > 430 nm > 409 nm. CO could inhibit the photo-oxidation process, indicating that the strength of the sixth coordination bond of Fe with a gas molecule influences the degree of photo-oxidation. The H⁺ and OH^- in the solution could also promote the photo-oxidation process. Irradiated by 254 and 280 nm light, free amino acids phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp) promoted the light oxidation reaction. Meanwhile, irradiation with 409 and 430 nm light had less influence on the UV-light-induced oxidation reaction under the same conditions. The results illustrated that in photo-induced oxidation of MbO₂, the formation of an excited state of Fe(Ⅱ) with unpaired electrons upon irradiation is crucial process for O₂ dissociation and Fe(Ⅱ) oxidation.

Key words: Oxymyoglobin, UV light, Free amino acid, Photo oxidation, Spectrometry

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Hong-Yu CAO,Ling-Xing GAO,Qian TANG,Jin-Hong SU,Xue-Fang ZHENG. Mechanism of Oxymyoglobin Oxidation Reaction Induced by Ultraviolet Light[J]. Acta Phys. -Chim. Sin. 2016, 32(4), 872-878. doi: 10.3866/PKU.WHXB201601046

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Mechanism of Oxymyoglobin Oxidation Reaction Induced by Ultraviolet Light

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