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 1.500&Aring;" /> '''P450CAM from Pseudo...)
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[[Image:2fe6.gif|left|200px]]<br /><applet load="2fe6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fe6.gif|left|200px]]<br /><applet load="2fe6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2fe6, resolution 1.500&Aring;" />
caption="2fe6, resolution 1.500&Aring;" />
'''P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX'''<br />
'''P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX'''<br />
==Overview==
==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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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==
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2FE6 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FE6 OCA].
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2FE6 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=2FE6 OCA].
==Reference==
==Reference==
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[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Koenig, K.von.]]
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[[Category: Koenig, K von.]]
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[[Category: Makris, T.M.]]
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[[Category: Makris, T M.]]
[[Category: Schlichting, I.]]
[[Category: Schlichting, I.]]
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[[Category: Sligar, S.G.]]
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[[Category: Sligar, S G.]]
[[Category: K]]
[[Category: K]]
[[Category: MNR]]
[[Category: MNR]]
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[[Category: substrate-free]]
[[Category: substrate-free]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:30:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:28 2008''

Revision as of 15:20, 21 February 2008


2fe6, resolution 1.500Å

Drag the structure with the mouse to rotate

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 and 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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