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  Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine

Aldag, C., Gromov, I. A., Garcia-Rubio, I., von König, K., Schlichting, I., Jaun, B., et al. (2009). Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine. Proceedings of the National Academy of Sciences of the United States of America, 106(14), 5481-5486. doi:10.1073/pnas.0810503106.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-3557-8 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-DB85-3
Genre: Journal Article

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 Creators:
Aldag, Caroline, Author
Gromov, Igar A., Author
Garcia-Rubio, Ines, Author
von König, Konstanze1, Author           
Schlichting, Ilme1, Author           
Jaun, Bernhard, Author
Hilvert, Donald, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: protein engineering; selenocysteine insertion; sequence element; selenoenzyme; stop codon suppression; X-ray crystallography
 Abstract: The unique monooxygenase activity of cytochrome P450cam has been attributed to coordination of a cysteine thiolate to the heme cofactor. To investigate this interaction, we replaced cysteine with the more electron-donating selenocysteine. Good yields of the selenoenzyme were obtained by bacterial expression of an engineered gene containing the requisite UGA codon for selenocysteine and a simplified yet functional selenocysteine insertion sequence (SECIS). The sulfur-to-selenium substitution subtly modulates the structural, electronic, and catalytic properties of the enzyme. Catalytic activity decreases only 2-fold, whereas substrate oxidation becomes partially uncoupled from electron transfer, implying a more complex role for the axial ligand than generally assumed.

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Language(s): eng - English
 Dates: 2008-10-172009-02-042009-03-172009-04-07
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.0810503106
URI: http://www.ncbi.nlm.nih.gov/pubmed/19293375
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 106 (14) Sequence Number: - Start / End Page: 5481 - 5486 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230