نتایج جستجو برای: quinol oxidation inhibitor
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The oxidative metabolism of irbesartan, a new nonpeptide angiotensin II receptor antagonist, was investigated on 12 human fully characterized hepatic microsomes and purified cytochrome P-450 (CYP) isoforms. After incubation of microsomes with irbesartan and NADPH, four main hydroxy metabolites were formed, as confirmed by liquid chromatography-mass spectrometry analysis. Irbesartan oxidation fo...
This review focuses on key components of respiratory and photosynthetic energy-transduction systems: the cytochrome bc1 b6f (Cytbc1/b6f) membranous multisubunit homodimeric complexes. These remarkable molecular machines catalyze electron transfer from quinones to water-soluble carriers (such as cytochromes c or plastocyanin), coupling flow proton translocation across energy-transducing membrane...
The striking resemblance of the rhombohedral and monoclinic forms of the title molecule to beta- and gamma-quinol provides a crystal engineering approach to new polymorphic systems.
Toluene dioxygenase-catalysed cis-dihydroxylation of phenols has led to the discovery of new enantiopure cyclohexenone cis-diol, o-quinol dimer and phenol hydrate metabolites having synthetic potential.
Background: Parkinson’s disease (PD) accompanies with degeneration of dopaminergic neurons of substantia nigra compacta and other regions of brainstem. Oxidative stress plays an important role in neuronal death in PD. Superoxide formation is one of the main etiologies of this disease, and angiotensin converting enzyme inhibitors (ACEIs) are able to suppress superoxide formation. Petroselinum...
The title compound, [Cu(2)(C(11)H(8)NO(3))(2)Cl(2)], is a bicopper(II) complex. Each Cu(II) ion is five-coordinated by two O atoms and one N atom from the (8-quinol-yloxy)acetate ligand, and by two μ(2)-chloride ligands, thus exhibiting a distorted square-pyramidal CuCl(2)NO(2) coordination environment. Each (8-quinol-yloxy)acetate anion acts as a tridentate chelating ligand. In the crystal str...
Native structures of ubihydroquinone:cytochrome c oxidoreductase (bc(1) complex) from different sources, and structures with inhibitors in place, show a 16-22 A displacement of the [2Fe-2S] cluster and the position of the C-terminal extrinsic domain of the iron sulfur protein. None of the structures shows a static configuration that would allow catalysis of all partial reactions of quinol oxida...
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