作者: Md. Selim , Arpita Sengupta Sadhu , Kalyan K. Mukherjea
DOI: 10.1007/S00706-010-0339-8
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摘要: Binding of chlorophyllin (Chln), a food-grade additive molecule with hemoglobin (Hb), has been studied by photophysical and photochemical methods view to unravel the biochemical transport pathway it. The binding affinity constant sites between Chln Hb are determined found be 3.3 × 105 M−1 15 (on tryptophan basis), respectively. Fluorimetric quenching experiments entail that is bound in vicinity residue Hb. Circular dichroism studies suggest induces change α-helical content Chlorophyllin hemoglobin, which confirmed from spectrofluorimetric studies, when fluorescence occurs because chlorophyllin-induced exposure hydrophillic zone. cyclic voltammetric indicate redox reaction FeII inhibited shielding it molecule.