Myoglobin with modified tetrapyrrole chromophores: binding specificity and photochemistry.

Stephanie Pröll, Brigitte Wilhelm, Bruno Robert, Hugo Scheer

Department Biologie I-Botanik, Universität München, Germany.

Biochimica et biophysica acta 2006 Jul

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Complexes were prepared of horse heart myoglobin with derivatives of (bacterio)chlorophylls and the linear tetrapyrrole, phycocyanobilin. Structural factors important for binding are (i) the presence of a central metal with open ligation site, which even induces binding of phycocyanobilin, and (ii) the absence of the hydrophobic esterifying alcohol, phytol. Binding is further modulated by the stereochemistry at the isocyclic ring. The binding pocket can act as a reaction chamber: with enolizable substrates, apo-myoglobin acts as a 13(2)-epimerase converting, e.g., Zn-pheophorbide a' (13(2)S) to a (13(2)R). Light-induced reduction and oxidation of the bound pigments are accelerated as compared to solution. Some flexibility of the myoglobin is required for these reactions to occur; a nucleophile is required near the chromophores for photoreduction (Krasnovskii reaction), and oxygen for photooxidation. Oxidation of the bacteriochlorin in the complex and in aqueous solution continues in the dark.

Citation

Stephanie Pröll, Brigitte Wilhelm, Bruno Robert, Hugo Scheer. Myoglobin with modified tetrapyrrole chromophores: binding specificity and photochemistry. Biochimica et biophysica acta. 2006 Jul;1757(7):750-63