2fe6
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(New page: 200px<br /><applet load="2fe6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fe6, resolution 1.500Å" /> '''P450CAM from Pseudo...)
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Revision as of 08:23, 21 November 2007
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P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX
Overview
The oxidative prowess of the P450 cytochromes in physiological reactions, is attributed to the production of a high-valent iron-oxo complex, or, Compound I intermediate, in the reaction cycle. Despite many years of, study, however, the full electronic description of this fleeting, intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450, oxo-Fe(IV) is examined and compared to analogous states in related heme, enzymes. In addition, the utilization of cofactor exchange to stabilize, high-valent oxo-states in the P450 is addressed. Structural and, spectroscopic studies on manganese reconstituted P450, and its, corresponding oxo-complex, are presented.
About this Structure
2FE6 is a Single protein structure of sequence from Pseudomonas putida with K and MNR as ligands. Active as Camphor 5-monooxygenase, with EC number 1.14.15.1 Full crystallographic information is available from OCA.
Reference
The status of high-valent metal oxo complexes in the P450 cytochromes., Makris TM, von Koenig K, Schlichting I, Sligar SG, J Inorg Biochem. 2006 Apr;100(4):507-18. Epub 2006 Feb 28. PMID:16510191
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