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

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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
OriginalsprogEngelsk
TidsskriftInternational Journal of Biological Macromolecules
Vol/bind51
Nummer3
Sider (fra-til)284-90
Antal sider7
ISSN0141-8130
DOI
StatusUdgivet - 2012

    Forskningsområder

  • neuroglobin

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Aktiviteter

  • University of Auckland

    Aktivitet: Besøg på en ekstern institution - typerBesøg ved en ekstern, akademisk institution

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