Heme-peptide/protein interactions: the binding of heme octa and undecapeptides, and microperoxidase-8 and -11, to human serum albumin.
The interaction of the heme octa (MP-8) and undeca (MP-11) peptides derived from cytochrome c with lipidated human serum albumin (HSA) has been investigated in aqueous solution. It is demonstrated that complex formation occurs in each case with a 1:1 stoichiometry. CN- binding has been used to investigate the accessibility of the heme in each complex by comparison with CN- interaction with methemalbumin. A preliminary study of the kinetics of the Fe3+MP-8/11 human serumalbumin (HSA) interaction demonstrates a clear ligand-size-related effect on mechanism of interaction--an ad hoc explanation of which is given in terms of HSA existing as two nonconverting conformers in solution.
Adams
P A
PA
Department of Chemical Pathology, University of Cape Town Medical School, Cape Province, Republic of South Africa.
Goold
R D
RD
Thumser
A A
AA
D003486:Cyanides / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism; D004227:Dithionite; D006420:Hemeproteins / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism
D003486:Cyanides; D003574:Cytochrome c Group; D006420:Hemeproteins; D012709:Serum Albumin; D004227:Dithionite; D010544:Peroxidases; C021799:microperoxidase