Abstract
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.
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Selected References
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- Cann J. R. Contribution of aromatic residue interactions to the stability of myoglobin. 3. Molecular complexes of aromatic compounds with hemin, hematoporphyrin, and myoglobin. Biochemistry. 1967 Nov;6(11):3435–3442. doi: 10.1021/bi00863a014. [DOI] [PubMed] [Google Scholar]
- Cann J. R. Contribution of aromatic residue interactions to the stability of myoglobin. II. Enhancement by aromatic compounds of the rate of urea denaturation. Biochemistry. 1967 Nov;6(11):3427–3434. doi: 10.1021/bi00863a013. [DOI] [PubMed] [Google Scholar]
- Cann J. R. Contribution of aromatic residue interactions to the stability of myoglobin. IV. Delineation of binding forces between aromatic compounds and myoglobin. Biochemistry. 1969 Oct;8(10):4036–4047. doi: 10.1021/bi00838a022. [DOI] [PubMed] [Google Scholar]
- KENDREW J. C. Side-chain interactions in myoglobin. Brookhaven Symp Biol. 1962 Dec;15:216–228. [PubMed] [Google Scholar]