Probing the Role of the Internal Disulfide Bond in Regulating Conformational Dynamics in Neuroglobin

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 2010 Jul 21

PMID 20643048

Citations 6

Authors

Luisana Astudillo

Sophie Bernad

Valerie Derrien

Pierre Sebban

Jaroslava Miksovska

Affiliations

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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.

Citing Articles

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