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关于铜(II)与芳香族氨基酸相互作用的红细胞沉降率和光吸收研究。

ESR and optical absorption studies on the copper (II) interaction with aromatic amino acids.

作者信息

Sportelli L, Neubacher H, Lohmann W

出版信息

Radiat Environ Biophys. 1976 Dec 23;13(4):305-13. doi: 10.1007/BF01331175.

DOI:10.1007/BF01331175
PMID:189347
Abstract

Electron spin resonance and optical absorption studies have been done in order to investigate the interaction between Cu2+ and aromatic amino acids in aqueous solution at 77 K and at room temperature as well. Depending on the concentration each aromatic amino acid can form two different kinds of complexes with Cu2+ which can be characterized by its ESR pattern. Additional information was obtained from optical d-d and CT transitions.

摘要

为了研究77K以及室温下Cu2+与水溶液中芳香族氨基酸之间的相互作用,进行了电子自旋共振和光吸收研究。根据浓度不同,每种芳香族氨基酸可与Cu2+形成两种不同类型的配合物,这可通过其电子自旋共振图谱来表征。从光学d-d跃迁和电荷转移跃迁中获得了更多信息。

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引用本文的文献

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ESR an optical absorption studies on the copper(II) interaction with small peptides containing aromatic amino acids.关于铜(II)与含芳香族氨基酸的小肽相互作用的电子自旋共振和光吸收研究。
Biophys Struct Mech. 1977 Sep 28;3(3-4):317-26. doi: 10.1007/BF00535704.

本文引用的文献

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Electron-Nuclear Double Resonance of a Protein That Contains Copper: Evidence for Nitrogen Coordination to Cu(II) in Stellacyanin.含铜蛋白质的电子-核双共振:紫铜氧化酶中氮与Cu(II)配位的证据。
Proc Natl Acad Sci U S A. 1970 Sep;67(1):79-86. doi: 10.1073/pnas.67.1.79.
2
INVESTIGATION OF THE IRON AND COPPER COMPLEXES OF AVIAN CONALBUMINS AND HUMAN TRANSFERRINS BY ELECTRON PARAMAGNETIC RESONANCE.通过电子顺磁共振对鸟类伴清蛋白和人类转铁蛋白的铁和铜配合物的研究。
Biochemistry. 1963 Nov-Dec;2:1341-5. doi: 10.1021/bi00906a028.
3
Magnetic resonance studies of copper(II)-triglycylglycine complexes.
铜(II)-三甘氨酰甘氨酸配合物的磁共振研究。
J Am Chem Soc. 1967 Nov 22;89(24):6071-7. doi: 10.1021/ja01000a014.
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Stereoelectronic properties of metalloenzymes. I. A comparison of the coordination of copper (II) in galactose oxidase and a model system, N,N'-ethylenebis(trifluoroacetylacetoniminato)copper(II).金属酶的立体电子性质。I. 半乳糖氧化酶中铜(II)的配位与模型体系N,N'-亚乙基双(三氟乙酰丙酮亚胺基)铜(II)的配位比较。
J Am Chem Soc. 1974 Feb 20;96(4):1019-23. doi: 10.1021/ja00811a012.
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