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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Skommer, J. Helbo, S. Henty, K. Brittain, T.
Description	Country affiliation: New Zealand Author Affiliation: Skommer J ( School of Biological Sciences, University of Auckland, Auckland, New Zealand.)
Abstract	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<1 mmHg. The ferrous form of the protein yields an oxygenated intermediate on reaction with oxygen. The rate of oxidation, by oxygen, follows a complex concentration dependence, consistent with the presence of two distinct oxidation mechanisms. A quantitative model for the two oxidation processes has been developed, which is consistent with a lowered distal histidine binding constant in the mutant form of the protein. These data suggest that the protein structure surrounding the heme site in neuroglobin limits access to external ligands and provides an energy barrier to the structural changes following ligand binding in this protein. However, the mutation does not appear to affect reactivity with cytochrome c and the anti-apoptotic activity of the mutant in human cells of neuronal origin is increased as compared to the wild type protein.
File Format	HTM / HTML
ISSN	01418130
Issue Number	3
Volume Number	51
e-ISSN	18790003
Journal	International Journal of Biological Macromolecules
Language	English
Publisher	Elsevier
Publisher Date	2012-10-01
Publisher Place	Netherlands
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Globins Chemistry Metabolism Mutant Proteins Nerve Tissue Proteins Apoptosis Drug Effects Carbon Monoxide Caspase 9 Cell Line Cytochromes c Enzyme Activation Pharmacology Heme Humans Ligands Oxidation-reduction Oxygen Protein Binding Protein Conformation Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology Biochemistry

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