Article
Trp180 of endothelial NOS and Trp56 of bacterial saNOS modulate sigma bonding of the axial cysteine to the heme.
Journal of inorganic biochemistry - 1 Jul 2009
Lang Jérôme, Driscoll Danelle, Gélinas Stéphanie, Rafferty Steven P, Couture Manon
Abstract excerpt
The proximal ligand of thiolate-coordinated heme proteins is crucial for the activation of the oxygen molecule and hydroxylation of substrates. In nitric oxide synthases (NOSs), the heme axial cysteine ligand forms a hydrogen bond to the side chain indole nitrogen of a tryptophan residue. Resonance Raman spectroscopy was used to probe W56F and W56Y variants of the NOS of Staphylococcus aureus (saNOS) and the...
Topics
- Animals
- Cloning, Molecular
- Cysteine
- Endothelium
- Heme
- Hydrogen Bonding
- Mutation
- Nitric Oxide
- Nitric Oxide Synthase Type III
- Spectrum Analysis, Raman
- Staphylococcus aureus