Proteins are a biochemical molecule that facilitates biological functions. One common protein includes myoglobin. Myoglobin is a protein of amino acids, containing an iron centered heme. The heme allows chemistry to take place with other small molecules as well as serving as an electron receiver and sender. The metal within the heme can be replaced with various metals such as cobalt, chromium and manganese. The ultimate goal is to replace manganese metal inside the heme group and react it with different oxidants to make myoglobin into an enzyme. Development of potential catalysts is beneficial for nitrene transfer and formation of new nitrogen compounds.  Manganese porphyrin was reacted with apomyoglobin, myoglobin without the heme group, forming manganese myoglobin. Manganese myoglobin was reacted with series of oxidants for possible reactions. Reactions occurred with nitrogen transfer agent, N(p-tosylsulfonyl)-imino-phenyliodoinane, and peroxide. Reactions were confirmed through changes of the ultraviolet spectrum and both oxidants formed similar spectrum due to the similar possible imido intermediate it formed. The kinetic of both reactions was then monitored, however only the nitrogen transfer agent exhibit identity of a catalyst because it produced an intermediate that reverted back to its original state. The peroxide reaction was stable and did not change back to its original form. This behavior by the nitrogen transfer agent confirms a possible catalytic reaction. This intermediate and catalytic behavior can aid to further finding in nitrene transfer.

Catalytic metal replaced myoglobin

243rd National Meeting (2012)

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