2qbm
From Proteopedia
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Crystal structure of the P450cam G248T mutant in the cyanide bound state
Overview
Distal pocket water molecules have been widely implicated in the delivery, of protons required in O-O bond heterolysis in the P450 reaction cycle., Targeted dehydration of the cytochrome P450cam (CYP101) distal pocket, through mutagenesis of a distal pocket glycine to either valine or, threonine results in the alteration of spin state equilibria, and has, dramatic consequences on the catalytic rate, coupling efficiency, and, kinetic solvent isotope effect parameters, highlighting an important role, of the active-site hydration level on P450 catalysis. Cryoradiolysis of, the mutant CYP101 oxyferrous complexes further indicates a specific, perturbation of proton-transfer events required for the transformation of, ferric-peroxo to ferric-hydroperoxo states. Finally, crystallography of, the 248Val and 248Thr mutants in both the ferric camphor bound resting, state and ferric-cyano adducts shows both the alteration of, hydrogen-bonding networks and the alteration of heme geometry parameters., Taken together, these results indicate that the distal pocket, microenvironment governs the transformation of reactive heme-oxygen, intermediates in P450 cytochromes.
About this Structure
2QBM is a Single protein structure of sequence from Pseudomonas putida with , , and as ligands. Active as Camphor 5-monooxygenase, with EC number 1.14.15.1 Full crystallographic information is available from OCA.
Reference
Alteration of P450 Distal Pocket Solvent Leads to Impaired Proton Delivery and Changes in Heme Geometry., Makris TM, Koenig KV, Schlichting I, Sligar SG, Biochemistry. 2007 Dec 11;46(49):14129-14140. Epub 2007 Nov 15. PMID:18001135
Page seeded by OCA on Wed Jan 23 11:27:17 2008
