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  The status of high-valent metal oxo complexes in the P450 cytochromes

Makris, T. M., von König, K., Schlichting, I., & Sligar, S. G. (2006). The status of high-valent metal oxo complexes in the P450 cytochromes. Journal of Inorganic Biochemistry, 100(4), 507-518. doi:10.1016/j.jinorgbio.2006.01.025.

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Genre: Journal Article
Alternative Title : The status of high-valent metal oxo complexes in the P450 cytochromes

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JInorgBiochem_100_2006_507.pdf (Any fulltext), 453KB
 
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 Creators:
Makris, Thomas M., Author
von König, Konstanze1, Author           
Schlichting, Ilme1, Author           
Sligar, Stephen G., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: P450; Compound I; Ferryl; Meta-Oxo; X-ray
 Abstract: 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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Language(s): eng - English
 Dates: 2006-01-172005-12-192006-01-172006-02-282006-04-01
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Journal of Inorganic Biochemistry
Source Genre: Journal
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Publ. Info: New York : Elsevier
Pages: - Volume / Issue: 100 (4) Sequence Number: - Start / End Page: 507 - 518 Identifier: ISSN: 0162-0134
CoNE: https://pure.mpg.de/cone/journals/resource/954925478535