Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm
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منابع مشابه
Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm.
Organisms have evolved elaborate systems that ensure the homeostasis of the thiol redox environment in their intracellular compartments. In Escherichia coli, the cytoplasm is kept under reducing conditions by the thioredoxins with the help of thioredoxin reductase and the glutaredoxins with the small molecule glutathione and glutathione reductase. As a result, disulfide bonds are constantly res...
متن کاملCatalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm.
Disulfide bond formation is a catalyzed process in vivo. In prokaryotes, the oxidation of cysteine pairs is achieved by the transfer of disulfides from the highly oxidizing DsbA/DsbB catalytic machinery to substrate proteins. The oxidizing power utilized by this system comes from the membrane-embedded electron transport system, which utilizes molecular oxygen as a final oxidant. Proofreading of...
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The zinc(II) complex [Zn2(dmdtc)2(μ-dmdtc)2] has been synthesized directly from thiram ligand, containing a disulfide bond {dmdtc = N,N-dimethyldithiocarbamate; thiram = N,N-tetramethylthiuram disulfide}, and characterized by elemental analysis and spectroscopic methods. Surprisingly thiram, undergoes a reductive disulfide bond scission upon reaction with Zn2+ in methanolic media to give the [Z...
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the zinc(ii) complex [zn2(dmdtc)2(μ-dmdtc)2] has been synthesized directly from thiram ligand, containing a disulfide bond {dmdtc = n,n-dimethyldithiocarbamate; thiram = n,n-tetramethylthiuram disulfide}, and characterized by elemental analysis and spectroscopic methods. surprisingly thiram, undergoes a reductive disulfide bond scission upon reaction with zn2+ in methanolic media to give the [z...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2009
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0812596106