ABSTRACT: Well-defined 1: 1 complexes have been formed between apomyoglobin (apoMb) and a number of chloro-phyllide derivatives. The chlorophyllides substitute for heme in the pocket of myoglobin. These include magnesium chlo-rophyllide a, magnesium and zinc pyrochlorophyllide a, zinc pyrochlorophyllide 6, zinc pyrochlorophyllide d, zinc pyro-mesochlorophyllide a, zinc 2-acetyl-2-devinylpyrochloroph yllide a, zinc protopyrochlorophyllide a, and zinc bacteriopyro-chlorophyllide a. The effects of the protein on the electronic absorption, circular dichroism (CD), magnetic circular di-chroism, and triplet state electron spin resonance spectra and fluorescence lifetimes in solution are compared with appro-priate models in organic solvents. With the exception of the CD spectra, the protein causes shifts and intensity changes which are within the range observed for solvent effects. The

Abstract not found