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          Institute: MPI für medizinische Forschung     Collection: Abteilung Biomolekulare Mechanismen     Display Documents



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ID: 472752.0, MPI für medizinische Forschung / Abteilung Biomolekulare Mechanismen
Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine
Translation of Title:Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine
Authors:Aldag, Caroline; Gromov, Igar A.; Garcia−Rubio, Ines; von König, Konstanze; Schlichting, Ilme; Jaun, Bernhard; Hilvert, Donald
Language:English
Date of Publication (YYYY-MM-DD):2009-04-07
Title of Journal:Proceedings of the National Academy of Sciences of the USA (JSTOR)
Journal Abbrev.:Proc. Natl. Acad. Sci. U. S. A.
Volume:106
Issue / Number:14
Start Page:5481
End Page:5486
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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.
Free Keywords:protein engineering; selenocysteine insertion; sequence element; selenoenzyme; stop codon suppression; X−ray crystallography
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
Identifiers:LOCALID:7497
URI:http%3A%2F%2Fwww.pnas.org%2Fcontent%2F106%2F14%2F5...
URI:http%3A%2F%2Fwww.pnas.org%2Fcontent%2F106%2F14%2F5...
URI:http%3A%2F%2Fwww.pnas.org%2Fcontent%2F106%2F14%2F5...
DOI:10.1073%2Fpnas.0810503106
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