Heme-linked proton dissociation of carbon monoxide complexes of myoglobin and peroxidase. - Suppr | 超能文献

Heme-linked proton dissociation of carbon monoxide complexes of myoglobin and peroxidase.

作者信息

Hayashi Y, Yamada H, Yamazaki I

出版信息

Biochim Biophys Acta. 1976 Apr 14;427(2):608-16. doi: 10.1016/0005-2795(76)90204-x.

DOI:10.1016/0005-2795(76)90204-x

PMID:5132

Abstract

It was found from spectrophotometric titration and proton balance measurement that the pKa value of a heme-linked protonation group of horseradish ferro-peroxidase C (donor:H2O2 oxidoreductase, EC 1.11.1.7) shifted from 7.25 to 8.25 upon combination with CO. The spectrophotometric titration experiment with myoglobin also revealed the presence of a heme-linked protonation group, the pKa value being 5.57 in myoglobin and 5.67 in the CO-myoglobin complex. It was concluded that the distinct shift of the pKa value in the case of peroxidase was attributable to the presence of a hydrogen bond between the sixth ligand and the distal base. The difference in the strength of such hydrogen bonding between peroxidase and myoglobin was discussed.

摘要

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Heme-linked proton dissociation of carbon monoxide complexes of myoglobin and peroxidase.

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Comparison of function of the distal base between myoglobin and peroxidase.

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Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon-13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes.通过一氧化碳配合物的碳-13核磁共振光谱比较过氧化物酶和其他血红素蛋白中的血红素环境和近端配体。

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[Contribution of protein conformation to stereochemistry and reactivity of the active center of heme proteins and enzymes. The existence of horseradish peroxidase conformations and their possible role in the catalysis mechanism].[蛋白质构象对血红素蛋白和酶活性中心的立体化学及反应性的贡献。辣根过氧化物酶构象的存在及其在催化机制中的可能作用]

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Infrared spectroscopic studies of carbonyl horseradish peroxidases.

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