A study of porphyrin analogues—III : Syntheses,enzyme interactions and self-aggregation of new models for types I,III and IX porphyrins |
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Authors: | Colin L. Honeybourne J.Timothy Jackson Derek J. Simmonds Owen T.G. Jones |
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Affiliation: | Physical Chemistry Laboratories, Bristol Polytechnic, Frenchay, Bristol, England |
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Abstract: | Three new porphyrin free bases have been synthesised and their interaction with the mitochondrial enzyme Ferrochelatase has been studied. The model compound for type IX porphyrins is the best substrate for Ferrochelatase so far studied, whereas the model compound for type I porphyrins is the only compound of this type to act as a substrate for this enzyme. The model compound for type III porphyrins is not a substrate, but does act as a competitive inhibitor.The 1H NMR spectra of the new compounds in their dimethyl diester form differ substantially from the spectra of their zinc(II)bis-pyrrolidine adducts, showing that aggregation is taking place. The results for the α-meso and γ-meso protons in particular are unusual and indicate that aggregation is taking place anomalously, with electronic effects dominating steric effects. |
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Keywords: | Present address: Department of Biochemistry The University of Bristol Bristol England. |
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