Contribution of aromatic residue interactions to the stability of myoglobin. V. Enhancement by aromatic compounds of the rate of heat denaturation.
Aromatic compounds like chlorpromazine and benzoate and its homologs strongly enhance the rate of heat denaturation of myoglobin. The latter apparently exert their action by complexing with a single kind of site in the hemeprotein. Both charge-transfer and hydrophobic interactions are implicated in complex formation, most probably with the heme moiety.
D000818:Animals; D001565:Benzoates; D001665:Binding Sites; D002591:Cetacea; D055598:Chemical Phenomena; D002621:Chemistry; D002746:Chlorpromazine; D006358:Hot Temperature; D007700:Kinetics; D009211:Myoglobin; D010654:Phenylbutyrates; D011422:Propionates; D011489:Protein Denaturation; D011726:Pyridinium Compounds; D014631:Valerates
D001565:Benzoates; D009211:Myoglobin; D010654:Phenylbutyrates; D011422:Propionates; D011726:Pyridinium Compounds; D014631:Valerates; D002746:Chlorpromazine