2fer: Difference between revisions

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[[Image:2fer.~~gif~~|left|200px]]

[[Image:2fer.png|left|200px]]

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~~'''~~P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX~~'''~~

===P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16510191}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16510191 is the PubMed ID number.

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==About this Structure==

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[[Category: Substrate-free]]

[[Category: Water cluster]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4~~ 03:48:42 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:14:17 2008''

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-[[Image:2fer.gif|left|200px]]
+{{Seed}}
+[[Image:2fer.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2fer|  PDB=2fer  |  SCENE=  }}
-'''P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16510191}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16510191 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16510191}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Substrate-free]]
 [[Category: Water cluster]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:48:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:14:17 2008''