Mercaptide-anion as a trans-ligand in oxycytochrome P450
| Autor: | M.F. Budyka, A.A. Shteinman, A.M. Khenkin |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Coordination sphere
Protein Conformation Biophysics Heme Sulfides Photochemistry Ligands Biochemistry law.invention chemistry.chemical_compound Cytochrome P-450 Enzyme System law Mössbauer spectroscopy Electron paramagnetic resonance Molecular Biology Transition metal dioxygen complex Magnetic circular dichroism Ligand Circular Dichroism Cell Biology chemistry Spectrophotometry Absorption (chemistry) Oxidation-Reduction Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 101(2) |
| ISSN: | 0006-291X |
| Popis: | Oxygenation of heme-mercaptide as well as spectroscopic characteristics of the dioxygen complex formed have been studied. Absorption and magnetic circular dichroism spectra of the O2 complex support the retention of mercaptide in the heme fifth position. A release of O2• in the decomposition of the oxygenated complex and an independent formation of the latter from hemine-dimercaptide and O2• together with electron paramagnetic resonance and Mossbauer data support the O2 presence in the heme coordination sphere. The similarity of optical and magnetic circular dichroism spectra and the closeness of the KCOKO2 ratio for oxy-heme-mercaptide and oxycytochrome P450 unequivocally confirm the presence of an axial cystein mercaptide ligand in oxycytochrome P450. |
| Databáze: | OpenAIRE |
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