5cp4
CRYOGENIC STRUCTURE OF P450CAM
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OverviewOverview
Proton transfer in cytochromes P450 is a critical step in the activation, of molecular oxygen. Extensive study of the P450cam active site has, identified several residues that play a central role in dioxygen bond, scission. A highly conserved carboxylate, aspartate-251 in P450cam in the, distal helix I, participates in a series of hydrogen-bond/ion pairs near, the molecular surface and has been implicated in the catalytic mechanism., Mutation of Asp251 is known to lower activity by 2 orders of magnitude and, change the rate-limiting step in the catalytic cycle, suggesting a role, for an acid functionality in generation of iron-oxygen reactive, intermediates. The turnover rates of the Asp251Asn mutant in various, protium-deuterium mixtures have been determined and show a significantly, ... [(full description)]
About this StructureAbout this Structure
5CP4 is a [Single protein] structure of sequence from [Pseudomonas putida] with K, HEM, CAM and GOL as [ligands]. Active as [Camphor 5-monooxygenase], with EC number [1.14.15.1]. Structure known Active Site: K. Full crystallographic information is available from [OCA].
ReferenceReference
Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect., Vidakovic M, Sligar SG, Li H, Poulos TL, Biochemistry. 1998 Jun 30;37(26):9211-9. PMID:9649301
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