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Dynamics of CO binding to heme proteins

โœ 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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๐Ÿ“œ SIMILAR VOLUMES


Femtosecond dynamics of heme proteins
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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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## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.

Steric contributions to CO binding in he
โœ Pawel M. Kozlowski; Kathleen M. Vogel; Marek Z. Zgierski; Thomas G. Spiro ๐Ÿ“‚ Article ๐Ÿ“… 2001 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 202 KB

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 effect of heterogeneous structural d
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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