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PrrC是来自球形红细菌的Sco同源物,具有硫醇-二硫键氧化还原酶活性。

PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity.

作者信息

Badrick Alison C, Hamilton Amanda J, Bernhardt Paul V, Jones Christopher E, Kappler Ulrike, Jennings Michael P, McEwan Alastair G

机构信息

Centre for Metals in Biology, School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Queensland 4072, Australia.

出版信息

FEBS Lett. 2007 Oct 2;581(24):4663-7. doi: 10.1016/j.febslet.2007.08.058. Epub 2007 Sep 4.

Abstract

PrrC is a Sco homologue in Rhodobacter sphaeroides that is associated with PrrBA, a two-component signal transduction system that induces photosynthesis gene expression in response to a decrease in oxygen tension. Although Sco proteins have been shown to bind copper the observation that they are structurally-related to thioredoxins suggested that they might possess thiol-disulfide oxidoreductase activity. Our results show that PrrC reduces Cu(2+) to Cu(+) and possesses disulfide reductase activity. These results indicate that some bacterial Sco proteins may have biochemical properties that are distinct from those of mitochondrial Sco proteins.

摘要

PrrC是球形红细菌中与PrrBA相关的Sco同源物,PrrBA是一种双组分信号转导系统,可响应氧张力降低诱导光合作用基因表达。尽管已证明Sco蛋白能结合铜,但它们在结构上与硫氧还蛋白相关这一观察结果表明,它们可能具有硫醇-二硫键氧化还原酶活性。我们的结果表明,PrrC可将Cu(2+)还原为Cu(+)并具有二硫键还原酶活性。这些结果表明,一些细菌Sco蛋白可能具有与线粒体Sco蛋白不同的生化特性。

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