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2
The formation of ferric haem during low-temperature photolysis of horseradish peroxidase Compound I.辣根过氧化物酶化合物I低温光解过程中高铁血红素的形成。
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本文引用的文献

1
Primary compounds of catalase and peroxidase.过氧化氢酶和过氧化物酶的主要化合物。
Biochem J. 1961 Feb;78(2):253-62. doi: 10.1042/bj0780253.
2
Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin.辣根过氧化物酶的纯化及其与过氧化氢酶和高铁血红蛋白性质的比较。
Biochem J. 1951 Jun;49(1):88-104. doi: 10.1042/bj0490088.
3
Magnetic properties of some peroxide compounds of myoglobin, peroxidase and catalase.肌红蛋白、过氧化物酶和过氧化氢酶的某些过氧化物化合物的磁性
Arch Biochem Biophys. 1952 Dec;41(2):442-61.
4
The spectra of the enzyme-substrate complexes of catalase and peroxidase.过氧化氢酶和过氧化物酶的酶-底物复合物光谱。
Arch Biochem Biophys. 1952 Dec;41(2):404-15. doi: 10.1016/0003-9861(52)90469-4.
5
Studies on cytochrome c peroxidase. I. Purification and some properties.细胞色素c过氧化物酶的研究。I. 纯化及某些性质
J Biol Chem. 1965 Nov;240(11):4503-8.
6
The electronic structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horseradish peroxidase and its derivatives.原血红素蛋白的电子结构。I. 辣根过氧化物酶及其衍生物的电子顺磁共振和光学研究。
J Biol Chem. 1968 Apr 25;243(8):1854-62.
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Mössbauer spectroscopic evidence for the electronic configuration of iron in horseradish peroxidase and its peroxide derivatives.
Biochemistry. 1969 Oct;8(10):4159-62. doi: 10.1021/bi00838a037.
8
Interaction of peroxidases with aromatic peracids and alkyl peroxides. Product analysis.过氧化物酶与芳族过酸和烷基过氧化物的相互作用。产物分析。
J Biol Chem. 1972 May 25;247(10):3353-60.
9
pH dependence of the oxidation of iodide by compound I of horseradish peroxidase.辣根过氧化物酶化合物I氧化碘化物的pH依赖性
Biochemistry. 1972 May 23;11(11):2076-82. doi: 10.1021/bi00761a013.
10
Photosensitization of small peptides by proflavine: an E.S.R. study at low temperature.硫酸原黄素对小肽的光敏化作用:低温下的电子自旋共振研究
Radiat Environ Biophys. 1974;11(3):239-45. doi: 10.1007/BF01323193.

辣根过氧化物酶化合物I光化学产生物种的电子顺磁共振研究。

Electron-paramagnetic-resonance studies on a photochemically produced species of horseradish peroxidase compound I.

作者信息

McIntosh A R, Stillman M J

出版信息

Biochem J. 1977 Oct 1;167(1):31-7. doi: 10.1042/bj1670031.

DOI:10.1042/bj1670031
PMID:201247
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1183618/
Abstract

Strong electron-paramagnetic-resonance signals in the g = 2.00 region were detected after irradiation of horseradish peroxidase Compound I at temperatures of 10 and 100 K. These signals establish the presence of new free-radical species in the peroxidase system. The new species are interpreted in terms of a haem-photosensitized oxidation of the protein's peptide groups close to the Compound I radical site. On warming to room temperature, the radicals decayed irreversibly to a species having a weak asymmetric electron-paramagnetic-resonance signal at 100 K, which could still be observed after incubation at room temperature for more than 1 h.

摘要

在10 K和100 K的温度下照射辣根过氧化物酶化合物I后,在g = 2.00区域检测到强电子顺磁共振信号。这些信号表明过氧化物酶系统中存在新的自由基物种。这些新物种被解释为靠近化合物I自由基位点的蛋白质肽基团的血红素光敏氧化。升温至室温后,自由基不可逆地衰减为在100 K时具有弱不对称电子顺磁共振信号的物种,在室温下孵育超过1小时后仍可观察到该信号。