Rheostat re-wired: alternative hypotheses for the control of thioredoxin reduction potentials

Thioredoxins are small soluble proteins that contain a redox-active disulfide (CXXC). These disulfides are tuned to oxidizing or reducing potentials depending on the function of the thioredoxin within the cell. The mechanism by which the potential is tuned has been controversial, with two main hypot...

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Veröffentlicht in:	PloS one 2015-04, Vol.10 (4), p.e0122466
Hauptverfasser:	Bewley, Kathryn D, Dey, Mishtu, Bjork, Rebekah E, Mitra, Sangha, Chobot, Sarah E, Drennan, Catherine L, Elliott, Sean J
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Archaea - chemistry Biochemistry Chemical bonds Correlation analysis Coupling (molecular) Crystallography Crystallography, X-Ray Denaturation Dependence E coli Fluorescence Fluorescent indicators Folding Glutathione - chemistry Glutathione - genetics Hydrogen bonds Hypotheses Mutagenesis, Site-Directed Oxidation Oxidation-Reduction pH effects Physiology Protein denaturation Protein Folding Proteins Redox potential Reduction Ribonucleotide reductase Thermodynamics Thioredoxin Thioredoxins - chemistry Thioredoxins - genetics Thioredoxins - metabolism X-ray crystallography
Online-Zugang:	Volltext
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