Issue 9, 2013
From the journal:

Dalton Transactions

Engineered metalloregulation of azide binding affinity and reduction potential of horse heart myoglobin

Christie L. Huntera  and  A. Grant Mauk*b  

* Corresponding authors

a AB SCIEX, Foster City, CA, USA

b Department of Biochemistry and Molecular and the Centre for Blood Research, University of British Columbia, Vancouver, BC, Canada
E-mail: grant.mauk@ubc.ca
Fax: +1 604-822-6860
Tel: +1 604-822-3719

Abstract

Metal ion binding to a previously reported variant of horse heart myoglobin (Lys45Glu/Lys63Glu) with a metal ion binding site on the surface of the protein that is adjacent to the haem binding site has been shown to influence ligand binding and electrochemical properties of the protein. For example, the Kd (μM) for binding of azide to this variant decreases from 277 ± 9 to 32 ± 3 following addition of a saturating concentration of Mn2+ (the value for the wild-type protein under the same conditions is 26 ± 1). Similarly, the midpoint reduction potential Em (mV vs. standard hydrogen electrode) increases from 9 to 40 in the presence of a saturating concentration of Mn2+ (the value for the wild-type protein under the same conditions is 45 ± 2). These results demonstrate the potential value of engineered metal ion binding sites as a means of regulating the functional properties of even simple haem proteins.

Graphical abstract: Engineered metalloregulation of azide binding affinity and reduction potential of horse heart myoglobin

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Article information

DOI
https://doi.org/10.1039/C2DT32558F
Article type
Paper
Submitted
25 Oct 2012
Accepted
06 Dec 2012
First published
06 Dec 2012

Dalton Trans., 2013,42, 3151-3155

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Engineered metalloregulation of azide binding affinity and reduction potential of horse heart myoglobin

C. L. Hunter and A. G. Mauk, Dalton Trans., 2013, 42, 3151 DOI: 10.1039/C2DT32558F

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