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Article Dans Une Revue Biochemistry Année : 2018

Development of a rubredoxin-type center embedded in a de novo designed three-helix bundle

Résumé

Protein design is a powerful tool to interrogate the basic requirements for the function of a metal site in a way that allows for the selective incorporation of elements important for function. Rubredoxins are small electron transfer proteins with a reduction potential centered near 0 mV (vs. NHE). All previous attempts at the design of a rubredoxin site have focused on incorporating the canonical CXXC motifs in addition to reproducing the peptide fold or using flexible loop regions to define the morphology of the site. We have produced a rubredoxin site in an utterly different fold, a three-helix bundle. This construct mimics the UV-visible, Mössbauer, EPR and magnetic circular dichroism spectra of native rubredoxin. Furthermore, the measured reduction potential suggests that this rubredoxin analogue could function similarly. Thus, we have shown that an α-helical scaffold sustains a rubredoxin site that can cycle with the desired potential between the Fe(II) and Fe(III) states and reproduces the spectroscopic characteristics of this electron transport protein without requiring the classic rubredoxin protein fold.

Dates et versions

hal-01761936 , version 1 (09-04-2018)

Identifiants

Citer

Alison G. Tebo, Tyler B. J. Pinter, Ricardo Garcia-Serres, Amy L. Speelman, Cédric Tard, et al.. Development of a rubredoxin-type center embedded in a de novo designed three-helix bundle. Biochemistry, 2018, 57 (16), pp.2308-2316. ⟨10.1021/acs.biochem.8b00091⟩. ⟨hal-01761936⟩
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