publication . Article . Other literature type . 2017

Probing Ligand Exchange in the P450 Enzyme CYP121 from Mycobacterium tuberculosis: Dynamic Equilibrium of the Distal Heme Ligand as a Function of pH and Temperature.

Andrew J. Fielding; Kednerlin Dornevil; Li Ma; Ian Davis; Aimin Liu;
Open Access
  • Published: 20 Nov 2017 Journal: Journal of the American Chemical Society, volume 139, pages 17,484-17,499 (issn: 0002-7863, eissn: 1520-5126, Copyright policy)
  • Publisher: American Chemical Society (ACS)
Abstract
CYP121 is a cytochrome P450 enzyme from Mycobacterium tuberculosis that catalyzes the formation of a C–C bond between the aromatic groups of its cyclodityrosine substrate (cYY). The crystal structure of CYP121 in complex with cYY reveals that the solvent-derived ligand remains bound to the ferric ion in the enzyme–substrate complex. Whereas in the generally accepted P450 mechanism, binding of the primary substrate in the active-site triggers the release of the solvent-derived ligand, priming the metal center for reduction and subsequent O2 binding. Here we employed sodium cyanide to probe the metal–ligand exchange of the enzyme and the enzyme–substrate complex. ...
Subjects
free text keywords: Colloid and Surface Chemistry, Biochemistry, General Chemistry, Catalysis, Ternary complex, Ligand, Stereochemistry, Cyanide, chemistry.chemical_compound, chemistry, Oxidoreductase, chemistry.chemical_classification, Heme, Adduct, Inorganic chemistry, Substrate (chemistry), Sodium cyanide, Article
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publication . Article . Other literature type . 2017

Probing Ligand Exchange in the P450 Enzyme CYP121 from Mycobacterium tuberculosis: Dynamic Equilibrium of the Distal Heme Ligand as a Function of pH and Temperature.

Andrew J. Fielding; Kednerlin Dornevil; Li Ma; Ian Davis; Aimin Liu;