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基于电子顺磁共振研究的亚硫酸盐氧化酶磷酸盐复合物的性质

The nature of the phosphate complex of sulphite oxidase from electron-paramagnetic-resonance studies.

作者信息

George G N, Prince R C, Kipke C A, Sunde R A, Enemark J H

机构信息

Exxon Research and Engineering, Annandale, NJ.

出版信息

Biochem J. 1988 Nov 15;256(1):307-9. doi: 10.1042/bj2560307.

Abstract

The phosphate complex of sulphite oxidase in the Mo(V) oxidation state was investigated by e.p.r. spectroscopy. Third-derivative spectra reveal a wealth of structural detail previously unobserved in this spectrum. Most notable is the presence of hyperfine coupling from two inequivalent I = 1/2 nuclei, which we tentatively attribute to two 31P nuclei. Unresolved hyperfine interactions from at least one exchangeable 1H nucleus are also present.

摘要

通过电子顺磁共振光谱对处于钼(V)氧化态的亚硫酸盐氧化酶的磷酸盐配合物进行了研究。三阶导数光谱揭示了此前在该光谱中未观察到的丰富结构细节。最显著的是存在来自两个不等价的I = 1/2核的超精细耦合,我们初步将其归因于两个31P核。还存在来自至少一个可交换1H核的未解析超精细相互作用。

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The reactions and the structures of molybdenum centers in enzymes.酶中钼中心的反应和结构。
Adv Enzymol Relat Areas Mol Biol. 1980;51:107-65. doi: 10.1002/9780470122969.ch3.
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The inorganic biochemistry of molybdoenzymes.钼酶的无机生物化学
Q Rev Biophys. 1988 Aug;21(3):299-329. doi: 10.1017/s0033583500004479.

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