Dynamics of CO binding to heme proteins
โ Scribed by Laura Eisenstein
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 537 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0020-7608
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๐ SIMILAR VOLUMES
The solution structure of polypeptides can now be achieved through NMR spectroscopy, as long as the molecular mass does not much exceed 40 000 Da [1][2][3][4][5]. The determination of the structure of heme proteins, however, requires the knowledge of the position of the iron and of the atoms of the
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Non-local Density Functional Theory (DFT) is applied to the calculation of geometry and vibrational frequencies of Fe^II^ (porphine)(imidazole)(CO), a model for CO adducts of heme proteins. Bond distances and angles are in agreement with crystallographic data, and frequencies are correctly calculate
The kinetics of ligand binding to heme proteins studied by flash photolysis display an algebraic time dependence at low temperatures in contrast exponential recombination observed under physiological conditions. This result shows that protein structures should be viewed as a tune average of intercon