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5cp4
From Proteopedia
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(New page: 200px<br /> <applet load="5cp4" size="450" color="white" frame="true" align="right" spinBox="true" caption="5cp4, resolution 1.75Å" /> '''CRYOGENIC STRUCTURE...)
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Revision as of 16:35, 29 October 2007
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CRYOGENIC STRUCTURE OF P450CAM
Overview
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 Structure
5CP4 is a [Single protein] structure of sequence from [Pseudomonas putida] with K, HEM, CAM and GOL as [ligands]. Active as [[1]], with EC number [1.14.15.1]. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Mon Oct 29 18:40:24 2007
Categories: Pseudomonas putida | Single protein | Li, H. | Poulos, T.L. | CAM | GOL | HEM | K | Electron transport | Heme enzyme | Monooxygenase | Oxidoreductase | P450
