Probing the role of the internal disulfide bond in regulating conformational dynamics in neuroglobin.

Biophysical Journal
Luisana AstudilloJaroslava Miksovská

Abstract

In this report, we demonstrate that the internal disulfide bridge in human neuroglobin modulates structural changes associated with ligand photo-dissociation from the heme active site. This is evident from time-resolved photothermal studies of CO photo-dissociation, which reveal a 13.4+/-0.9 mL mol(-1) volume expansion upon ligand photo-release from human neuroglobin, whereas the CO dissociation from rat neuroglobin leads to a significantly smaller volume change (DeltaV=4.6+/-0.3 mL mol(-1)). Reduction of the internal disulfide bond in human neuroglobin leads to conformational changes (reflected by DeltaV) nearly identical to those observed for rat Ngb. Our data favor the hypothesis that the disulfide bond between Cys46 and Cys55 modulates the functioning of human neuroglobin.

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Citations

Nov 9, 2012·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Anthony BocahutEwen Lescop
Nov 9, 2016·Molecular Aspects of Medicine·Paolo AscenziMaria Marino
Apr 4, 2014·Chemical Reviews·Luisa B Maia, José J G Moura
Jun 5, 2013·Physical Chemistry Chemical Physics : PCCP·Stefania AbbruzzettiCristiano Viappiani
Apr 5, 2014·Acta Crystallographica. Section D, Biological Crystallography·Beatriz G GuimarãesBéatrice Golinelli-Pimpaneau
Jul 22, 2018·Dalton Transactions : an International Journal of Inorganic Chemistry·Hai-Xiao LiuYing-Wu Lin
Feb 5, 2021·Inorganic Chemistry·Shun-Fa ChenYing-Wu Lin
Feb 7, 2018·Archives of Biochemistry and Biophysics·Ying-Wu Lin
Oct 28, 2017·Journal of Inorganic Biochemistry·Marzia BelleiGianantonio Battistuzzi
May 27, 2014·Journal of Chemical Information and Modeling·Alexander N MorozovDavid C Chatfield

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