Relaxation of the folding of globulin around heme of hemoglobin of Homo sapiens by the food-grade additive molecule chlorophyllin

Abstract  

Binding of chlorophyllin (Chln), a food-grade additive molecule with hemoglobin (Hb), has been studied by photophysical and photochemical methods with a view to unravel the biochemical transport pathway of it. The binding affinity constant and binding sites between Chln and Hb are determined and found to be 3.3 × 10⁵ M⁻¹ and 15 (on tryptophan basis), respectively. Fluorimetric quenching experiments entail that Chln is bound in the vicinity of the tryptophan residue of Hb. Circular dichroism studies suggest that Chln induces a change in the α-helical content of Hb. Chlorophyllin is bound in the vicinity of the tryptophan residue of hemoglobin, which has been confirmed from spectrofluorimetric studies, when a quenching in the tryptophan fluorescence occurs because of the chlorophyllin-induced exposure of the tryptophan residue to hydrophillic zone. The cyclic voltammetric studies indicate that the redox reaction of Fe^II of Hb is inhibited shielding of it by the Chln molecule.