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谷胱甘肽配位的金属配合物作为细胞转运体的底物。

Glutathione-coordinated metal complexes as substrates for cellular transporters.

机构信息

The Ohio State University Biophysics Program, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210, USA.

Department of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA.

出版信息

Metallomics. 2021 Apr 30;13(5). doi: 10.1093/mtomcs/mfab015.

Abstract

Glutathione is the major thiol-containing species in both prokaryotes and eukaryotes and plays a wide variety of roles, including detoxification of metals by sequestration, reduction, and efflux. ABC transporters such as MRP1 and MRP2 detoxify the cell from certain metals by exporting the cations as a metal-glutathione complex. The ability of the bacterial Atm1 protein to efflux metal-glutathione complexes appears to have evolved over time to become the ABCB7 transporter in mammals, located in the inner mitochondrial membrane. No longer needed for the role of cellular detoxification, ABCB7 appears to be used to transport glutathione-coordinated iron-sulfur clusters from mitochondria to the cytosol.

摘要

谷胱甘肽是原核生物和真核生物中主要的含巯基物质,具有广泛的功能,包括通过螯合、还原和外排来解毒金属。ABC 转运蛋白,如 MRP1 和 MRP2,通过将阳离子作为金属-谷胱甘肽复合物输出,从细胞中解毒某些金属。细菌 Atm1 蛋白将金属-谷胱甘肽复合物排出细胞的能力似乎随着时间的推移而进化,成为哺乳动物中的 ABCB7 转运蛋白,位于线粒体内膜。由于不再需要细胞解毒的作用,ABCB7 似乎被用于将谷胱甘肽协调的铁硫簇从线粒体运输到细胞质。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/be06/8716071/d1196175dfab/mfab015gra.jpg

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