Ligand binding, reactivity and biological activity of a distal pocket mutant of neuroglobin

TY - JOUR

T1 - Ligand binding, reactivity and biological activity of a distal pocket mutant of neuroglobin

AU - Skommer, J

AU - Helbo, Signe

AU - Henty, K

AU - Brittain, T

N1 - Copyright © 2012 Elsevier B.V. All rights reserved.

PY - 2012

Y1 - 2012

N2 - We have generated the Lys67Glu mutant form of neuroglobin. Experimental spectral studies are consistent with a six coordinate heme in which the distal histidine bond is stretched compared to the wild type protein. Carbon monoxide binding to the ferrous form of the mutant follows a hyperbolic concentration dependence limiting at the histidine dissociation rate of 0.7 s(-1). Further analysis indicates a significantly lowered histidine binding constant. Oxygen binding kinetic studies confirm the higher heme ligand dissociation level and indicate a p50 value for oxygen binding

AB - We have generated the Lys67Glu mutant form of neuroglobin. Experimental spectral studies are consistent with a six coordinate heme in which the distal histidine bond is stretched compared to the wild type protein. Carbon monoxide binding to the ferrous form of the mutant follows a hyperbolic concentration dependence limiting at the histidine dissociation rate of 0.7 s(-1). Further analysis indicates a significantly lowered histidine binding constant. Oxygen binding kinetic studies confirm the higher heme ligand dissociation level and indicate a p50 value for oxygen binding

KW - neuroglobin

U2 - 10.1016/j.ijbiomac.2012.05.020

DO - 10.1016/j.ijbiomac.2012.05.020

M3 - Journal article

C2 - 22634514

SN - 0141-8130

VL - 51

SP - 284

EP - 290

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

IS - 3

ER -