Probing the role of the internal disulfide bond in regulating conformational dynamics in neuroglobin.
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.
Astudillo
Luisana
L
Bernad
Sophie
S
Derrien
Valérie
V
Sebban
Pierre
P
Miksovska
Jaroslava
J
D000818:Animals; D002151:Calorimetry; D002248:Carbon Monoxide / Q000737:chemistry; D004220:Disulfides / Q000378:metabolism*; D005914:Globins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism*; D000078787:Neuroglobin; D011487:Protein Conformation; D051381:Rats; D013057:Spectrum Analysis
D004220:Disulfides; D009419:Nerve Tissue Proteins; D000078787:Neuroglobin; D002248:Carbon Monoxide; D005914:Globins