Linear free energy relationships in binding of oxygen and carbon monoxide with heme model compounds and heme proteins
✍ Scribed by D. Lavalette; C. Tétreau; J. Mispelter; M. Momenteau; J.M. Lhoste
- Book ID
- 115122823
- Publisher
- John Wiley and Sons
- Year
- 1984
- Tongue
- English
- Weight
- 285 KB
- Volume
- 145
- Category
- Article
- ISSN
- 1432-1327
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## Abstract Second derivative absorption spectra are reported for the __aa__~3~‐cytochrome __c__ oxidase from bovine cardiac mitochondria, the __aa__~3~‐600 ubiquinol oxidase from __Bacillus subtilis__, the __ba__~3~‐cytochrome __c__ oxidase from __Thermus thermophilis__, and the __aco__‐cytochrome
13C- and 57Fe-NMR spectra of several carbon monoxide hemoprotein models with varying polar and steric effects of the distal organic superstructure, constraints of the proximal side, and solvent polarity are reported. The 13C shieldings of heme models cover a 4.0 ppm range that is extended to 7.0 ppm