对黄嘌呤氧化酶进行的电子-电子双共振测量。

Electron-electron double resonance measurements on xanthine oxidase.

作者信息

Lowe D J, Hyde J S

出版信息

Biochim Biophys Acta. 1975 Jan 23;377(1):205-10. doi: 10.1016/0005-2744(75)90302-2.

DOI:10.1016/0005-2744(75)90302-2

Abstract

Electron-electron double resonance measurements were carried out on milk xanthine oxidase (xanthine:oxygen oxidoreductase EC 1.2.3.2) and the spectra obtained supported a previous model, based on EPR data, proposing a spin-spin interaction between unpaired electrons associated with Fe-S and Mo. The technique demonstrated that the additional apparently isotropic, splitting in the Mo EPR spectra observed at low temperature is produced by a single site giving two spectra interconverting at a rate consistent with the Fe-S spin lattice relaxation time. Other data concerning the model and the relaxation behaviour of the species are discussed.

摘要

对牛奶黄嘌呤氧化酶（黄嘌呤：氧氧化还原酶，EC 1.2.3.2）进行了电子 - 电子双共振测量，所得光谱支持了基于电子顺磁共振（EPR）数据的先前模型，该模型提出与铁硫簇（Fe-S）和钼相关的未成对电子之间存在自旋 - 自旋相互作用。该技术表明，在低温下观察到的钼EPR光谱中额外的明显各向同性分裂是由一个单一位置产生的，该位置给出两个以与铁硫簇自旋晶格弛豫时间一致的速率相互转换的光谱。还讨论了有关该模型和该物种弛豫行为的其他数据。

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Magnetic coupling of the molybdenum and iron-sulphur centres in xanthine oxidase and xanthine dehydrogenases.黄嘌呤氧化酶和黄嘌呤脱氢酶中钼与铁硫中心的磁耦合

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