In order to investigate heme proteins, cofactor exchange is an emerging method.[1,2,3] Extracting the native heme cofactor leads to the apoprotein, which can be reconstituted with an artificial heme-analog molecule afterwards. Apart from modified porphyrins, other tetrapyrroles like phthalocyanine, porphycene and corrole have been used.[2,3,4] The corrole macrocycle can stabilize higher metal oxidation states[5] and the biohybrid proteins therefore exhibit interesting properties.[6,7] Here the synthesis and spectroscopic characterization of biomimetic iron and manganese corroles is shown. These were incorporated into heme proteins as non-natural cofactors and the biohybrid compounds were investigated by UV-Vis, EPR, HR-ESI-MS and other methods. References:[1] Y. Lu, S. M. Berry, T. D. Pfister, Chem. Rev. 2001 , 101, 3047�3080.[2] L. Fruk, C.-H. Kuo, E. Torres, C. Niemeyer, Angew. Chem. Int. Ed. 2009 , 48, 1550-1574.[3] T. Hayashi, Y. Hisaeda, Acc. Chem. Res. 2002 , 35, 35-43.[4] T. Matsuo, A. Hayashi, M. Abe, T. Matsuda, Y. Hisaeda, T. Hayashi, J. Am. Chem. Soc. 2009 , 131, 15124-15125.[5] I. Aviv-Harel, Z. Gross, Chem. Eur. J. 2009 , 15, 8382-8394.[6] M. Br�ring, F. Br�gier, O. Burghaus, C. Kleeberg, Z. Anorg. Allg. Chem. 2010 , 636, 1760-1766.[7] B. Gisk, F. Br�gier, R. A: Kr�ger, M. Br�ring, N. Frankenberg-Dinkel, Biochemistry 2010 , 49, 10042-10044.

Biomimetic corroles: Spectroscopic characterization and reconstitution with apomyoglobin

248th National Meeting (2014)

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