| Autor: |
Howes BD; Dipartimento di Chimica, Università di Firenze, 50121 Firenze, Italy., Schiodt CB, Welinder KG, Marzocchi MP, Ma JG, Zhang J, Shelnutt JA, Smulevich G |
| Jazyk: |
angličtina |
| Zdroj: |
Biophysical journal [Biophys J] 1999 Jul; Vol. 77 (1), pp. 478-92. |
| DOI: |
10.1016/S0006-3495(99)76905-5 |
| Abstrakt: |
Electronic absorption and resonance Raman (RR) spectra of the ferric form of barley grain peroxidase (BP 1) at various pH values, at both room temperature and 20 K, are reported, together with electron paramagnetic resonance spectra at 10 K. The ferrous forms and the ferric complex with fluoride have also been studied. A quantum mechanically mixed-spin (QS) state has been identified. The QS heme species coexists with 6- and 5-cHS hemes; the relative populations of these three spin states are found to be dependent on pH and temperature. However, the QS species remains in all cases the dominant heme spin species. Barley peroxidase appears to be further characterized by a splitting of the two vinyl stretching modes, indicating that the vinyl groups are differently conjugated with the porphyrin. An analysis of the currently available spectroscopic data for proteins from all three peroxidase classes suggests that the simultaneous occurrence of the QS heme state as well as the splitting of the two vinyl stretching modes is confined to class III enzymes. The former point is discussed in terms of the possible influences of heme deformations on heme spin state. It is found that moderate saddling alone is probably not enough to cause the QS state, although some saddling may be necessary for the QS state. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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