Interaction of haemoglobin and cytochrome c with aliphatic alcohols as studied by 1H NMR spectroscopy.
Association of haeme proteins, haemoglobin and cytochrome c, with eight aliphatic alcohols (methanol, ethanol. two isomeric propanols and four butanols) was studied by 1H NMR spectroscopy. NMR spectra of alcohols were monitored at 60 MHz at increasing concentration of the proteins. Selective broadening of the NMR signals of individual segments of alcohols was observed only in the case of alcohol-haemoglobin systems. Its quantitative evaluation and interpretation in terms of formation of low affinity intermolecular alcohol--protein complexes led to the conclusion that haemoglobin associates with alcohol molecules in a way depending on the length and isomeric branching of the alkyl chains; in particular, the methylene and methine groups vicinal to the hydroxyl are subject to stronger immobilization than the terminal methyls or other groups. Thus, the model of hydrophobic complexes stabilized by hydrogen bonds described previously for association of bovine serum albumin with alcohols (Lubas et al., Biochemistry, 18, 4943-4951, 1979) seems to apply also to haemoglobin association. In the case of cytochrome c association, 1H NMR data alone are insufficient for structural evaluation of the mechanism of formation of the alcohol--cytochrome c complexes.
D000438:Alcohols / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D003574:Cytochrome c Group / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D011485:Protein Binding; D011489:Protein Denaturation
D000438:Alcohols; D003574:Cytochrome c Group; D006454:Hemoglobins