IntroductionOurworkisaimedatmakinghybridmyoglobinsto.pptVIP

Introduction Our work is aimed at making hybrid myoglobins to use in photochemical studies of catalysis by heme proteins. Although myoglobin does not perform enzymatic functions in vivo, catalytically active analogues can be synthesized via the modification of the heme group (porphyrin) with a photoactive ruthenium bpy pendant arm. Reconstitution of these into apomyoglobin serves as a model for the catalytically active heme proteins. ;Synthesis of Bpy Pendant Arm; ;Metallation of Heme Cofactor;Preparation of Apomyoglobin;Molecular Model of Hybrid Mb;Wavelength (nm);LASER;Photoinduced nanosecond transient absorption;Future Work During the next year we will attempt to reconstitute the RuC7FePP heme cofactor into CcP. In myoglobin the active site is located on the edge of the protein whereas in CcP one of the propionate groups is blocked and the other is recessed from the periphery of the protein. Due to the topographic differences in the active sites, it is probable that we will need to alter the length and characteristics of the pendant arm in order for successful reconstitution. Other Possible Pendant Groups: -Re(bpy)(CO)3L (L= Cl-, Br-, pyridine) -Methyl viologen ;Acknowledgments