Studies on the hemeproteins, hemoglobin, myoglobin, catalase, peroxidase and cytochrome P-450 will be carried out in order to determine the mechanisms of action of oxygen storage, transport and activation and the mechanisms of electron transport. These enzymes and simple metalloporphyrins will be studied using electrochemical, kinetic, optical and magnetic resonance techniques. The goals are an understanding of the structural and electronic effects which govern the proper functioning of these proteins, as well as the causes and effects of their misfunctioning such as with abnormal hemoglobins and heptatic destruction of P-450 by unsaturated xenobiotics.
| Dolphin, D (1988) The generation of radicals during the normal and abnormal functioning of cytochromes P-450. Basic Life Sci 49:491-500 |
| David, S; James, B R; Dolphin, D (1986) Durene-capped porphyrin complexes of iron(II). Binding of imidazoles, and spectroscopic trends within Fe(porp)B(L) species (B = imidazole base;L = RNC, CO, O2). J Inorg Biochem 28:125-35 |
| Dolphin, D (1985) Cytochrome P450: substrate and prosthetic-group free radicals generated during the enzymatic cycle. Philos Trans R Soc Lond B Biol Sci 311:579-91 |
| Wijesekera, T P; Dolphin, D (1985) Some preparations and properties of porphyrins. Adv Exp Med Biol 193:229-66 |
