2fe6

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{{STRUCTURE_2fe6| PDB=2fe6 | SCENE= }}
{{STRUCTURE_2fe6| PDB=2fe6 | SCENE= }}
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'''P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX'''
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===P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16510191 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16510191}}
==About this Structure==
==About this Structure==
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[[Category: Mono-oxygenase]]
[[Category: Mono-oxygenase]]
[[Category: Substrate-free]]
[[Category: Substrate-free]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:47:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:51:38 2008''

Revision as of 05:51, 29 July 2008

Image:2fe6.png

Template:STRUCTURE 2fe6

P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX

Template:ABSTRACT PUBMED 16510191

About this Structure

2FE6 is a Single protein structure of sequence from Pseudomonas putida. 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

Page seeded by OCA on Tue Jul 29 08:51:38 2008

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