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鉴定涉及铁氧还蛋白和铁氧还蛋白:NADP 还原酶的共价连接复合物。

Characterization of a covalently linked complex involving ferredoxin and ferredoxin: NADP reductase.

机构信息

Department of Chemistry and Biochemistry, University of Arkansas, 72701, Fayetteville, AR, USA.

出版信息

Photosynth Res. 1988 Sep;17(3):231-45. doi: 10.1007/BF00035450.

Abstract

Ferredoxin and the flavoprotein, ferredoxin: NADP reductase, have been covalently linked by incubation in the presence of a water soluble carbodiimide. The cross-linking reaction yields an adduct having a 1:1 stoichiometry. The adduct has depressed levels of diaphorase and NADPH oxidase activity and is inactive in reduction of cytochrome c using NADPH as an electron donor. Thus, although similar to an adduct described by Zanetti and coworkers [J Biol Chem 259: 6153-6157 (1984)] in its stoichiometry, the adduct described herein has significantly different enzymatic properties. It is suggested that this may be a reflection of differences in the interaction between the two proteins resulting from differences in experimental conditions in which the two adducts were prepared.

摘要

铁氧还蛋白和黄素蛋白,铁氧还蛋白:NADP 还原酶,通过在水溶性碳二亚胺存在下孵育而共价连接。交联反应生成具有 1:1 化学计量的加合物。加合物的二氢还蛋白和 NADPH 氧化酶活性降低,并且在用 NADPH 作为电子供体还原细胞色素 c 时无活性。因此,尽管与 Zanetti 等人描述的加合物[J Biol Chem 259:6153-6157(1984)]在化学计量上相似,但本文描述的加合物具有明显不同的酶学性质。这可能反映了由于两种加合物制备条件的不同,两种蛋白质之间的相互作用存在差异。

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