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• W1983560601 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 K(d) (μM) for binding of azide to this variant decreases from 277 ± 9 to 32 ± 3 following addition of a saturating concentration of Mn(2+) (the value for the wild-type protein under the same conditions is 26 ± 1). Similarly, the midpoint reduction potential E(m) (mV vs. standard hydrogen electrode) increases from 9 to 40 in the presence of a saturating concentration of Mn(2+) (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." @default.
• W1983560601 created "2016-06-24" @default.
• W1983560601 creator A5076881039 @default.
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• W1983560601 date "2013-01-01" @default.
• W1983560601 modified "2023-09-25" @default.
• W1983560601 title "Engineered metalloregulation of azide binding affinity and reduction potential of horse heart myoglobin" @default.
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• W1983560601 doi "https://doi.org/10.1039/c2dt32558f" @default.
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