Direct electrochemical analyses of a thermophilic thioredoxin reductase: interplay between conformational change and redox chemistry.

Biochemistry
Michael J HamillSean J Elliott

Abstract

Thioredoxin reductases (TrxRs) are flavin-containing dithioloxidoreductases that couple reduction equivalents from the soluble NAD(P)H pool to the soluble protein thioredoxin (Trx). Previous crystallographic studies of the Escherichia coli enzyme ( ecTrxR) have shown that low molecular weight TrxRs can adopt two distinct conformations: the first (FO) is required for the oxidation of the flavin cofactor and the generation of reduced Trx; the second (FR) is adopted for the reduction of the flavin by NAD(P)H. Here, protein electrochemistry has been used to interrogate the equilibrium between the oxidized and reduced conformations of the ecTrxR and a novel, low molecular weight TrxR from the thermophilic archaeon Thermoplasma acidophilum ( taTrxR) that is characterized structurally and biochemically in the accompanying paper [Hernandez et al. (2008) Biochemistry 47, 9728-9737]. A reversible electrochemical response is observed that reveals a dynamic behavior dependent upon the temperature of the experiment. At low temperatures (283 K) a broad, quasi-reversible electrochemical envelope is observed centered at a value of approximately -300 mV and displaying a peak width of over 150 mV. The voltammetric response sharpens dramatically ...Continue Reading

References

Jan 1, 1985·Annual Review of Biochemistry·A Holmgren
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Sep 30, 2000·European Journal of Biochemistry·E S Arnér, A Holmgren
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Jul 16, 2008·Chemical Reviews·Christophe Léger, Patrick Bertrand
Aug 23, 2008·Biochemistry·Hector H HernandezCatherine L Drennan

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Citations

Jul 29, 2011·Chemical Reviews·Zhiyong ChengCharles H Williams
Jan 16, 2016·Biochimica Et Biophysica Acta·Américo G DuarteInês A C Pereira
Oct 30, 2016·The Journal of Biological Chemistry·Dwi SusantiBiswarup Mukhopadhyay
Aug 23, 2008·Biochemistry·Hector H HernandezCatherine L Drennan

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