Metal-replaced hemoproteins have been examined by biochemists for their functionality, but have not been thoroughly investigated.  By replacing hemoproteins with non-native metals, heme-containing proteins could be capable of performing a range of chemistries not allowed for in the native protein.  The metal within the heme of the oxygen-carrying hemoprotein, myoglobin, can readily be replaced with other first row transition metals such as cobalt, chromium and manganese.  Manganese-replaced myoglobin is the focus of this study since manganese does not bind dioxygen in air for ease of experimentation with undergraduate researchers.  We have discovered that the new myoglobin has some interesting oxygen transfer and hydrogen atom abstraction abilities when reacted with two-electron oxidants (meta-chloroperbenzoic acid) and with the addition of suitable substrates.  By replacement of the metal ion at the active site of myoglobin, we have effectively turned an oxygen-carrying protein into one that has unusual reactivities.

Metal-replaced myoglobin to promote new reactivities

246th National Meeting (2013)

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