2fer: Difference between revisions
New page: left|200px<br /><applet load="2fer" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fer, resolution 1.70Å" /> '''P450CAM from Pseudom... |
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[[Image:2fer.gif|left|200px]]<br /><applet load="2fer" size=" | [[Image:2fer.gif|left|200px]]<br /><applet load="2fer" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2fer, resolution 1.70Å" /> | caption="2fer, resolution 1.70Å" /> | ||
'''P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX'''<br /> | '''P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX'''<br /> | ||
==Overview== | ==Overview== | ||
The oxidative prowess of the P450 cytochromes in physiological reactions | 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== | ==About this Structure== | ||
2FER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with K and MNR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] Full crystallographic information is available from [http:// | 2FER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=MNR:'>MNR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FER OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Koenig, K | [[Category: Koenig, K von.]] | ||
[[Category: Makris, T | [[Category: Makris, T M.]] | ||
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
[[Category: Sligar, S | [[Category: Sligar, S G.]] | ||
[[Category: K]] | [[Category: K]] | ||
[[Category: MNR]] | [[Category: MNR]] | ||
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[[Category: water cluster]] | [[Category: water cluster]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:38 2008'' | ||
Revision as of 18:20, 21 February 2008
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P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX
OverviewOverview
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 StructureAbout this Structure
2FER 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.
ReferenceReference
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 Thu Feb 21 17:20:38 2008