Resonance Raman study on yeast cytochrome c peroxidase Effect of coordination and axial ligands
✍ Scribed by Gunnel Sievers; Kaj Österlund; Nils Ellfolk
- Book ID
- 113126137
- Publisher
- Elsevier Science
- Year
- 1979
- Weight
- 692 KB
- Volume
- 581
- Category
- Article
- ISSN
- 0005-2795
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Time-resolved resonance Raman spectroscopic measurements were undertaken to probe the axial ligand and solvent effects on the photophysical and photochemical processes of some paramagnetic metalloporphyrins (Cu II , Cr III , Mn III and Fe III porphyrins). The presence of odd electrons in d-orbitals
The addition of exogenous ligands to the ferric and ferrous states of yeast cytochrome c peroxidase (CCP) is investigated with magnetic circular dichroism (MCD) at 4°C to determine the effect the protein environment may exercise on spectral properties. The MCD spectrum of each derivative is directly
## Abstract __The effect on the heme environment upon unfolding__ Paracoccus versutus __ferricytochrome c‐550 and two site‐directed variants, K99E and H118Q, has been assessed through a combination of peroxidase activity increase and one‐dimensional NMR spectroscopy. At pH 4.5, the data are consist