Journal article
Structure of a de novo designed protein model of radical enzymes
Journal of the American Chemical Society, Vol.124(37), pp.10952-10953
09/18/2002
DOI: 10.1021/ja0264201
PMID: 12224922
Abstract
The use of side chains as catalytic cofactors for protein mediated redox chemistry raises significant mechanistic issues as to how these amino acids are activated toward radical chemistry in a controlled manner. De novo protein design has been used to examine the structural basis for the creation and maintenance of a tryptophanyl radical in a three-helix bundle protein maquette. Here we report the detailed structural analysis of the protein by multidimensional NMR methods. An interesting feature of the structure is an apparent pi-cation interaction involving the sole tryptophan and a lysine side chain. Hybrid density functional calculations support the notion that this interaction raises the reduction potential of the W degrees /WH redox pair and helps explain the redox characteristics of the protein. This model protein system therefore provides a powerful model for exploring the structural basis for controlled radical chemistry in protein.
Details
- Title: Subtitle
- Structure of a de novo designed protein model of radical enzymes
- Creators
- Qing-Hong Dai - The Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USACecilia TommosErnesto J FuentesMargareta R A BlombergP Leslie DuttonA Joshua Wand
- Resource Type
- Journal article
- Publication Details
- Journal of the American Chemical Society, Vol.124(37), pp.10952-10953
- Publisher
- United States
- DOI
- 10.1021/ja0264201
- PMID
- 12224922
- ISSN
- 0002-7863
- eISSN
- 1520-5126
- Grant note
- GM48130 / NIGMS NIH HHS GM35940 / NIGMS NIH HHS
- Language
- English
- Date published
- 09/18/2002
- Academic Unit
- Biochemistry and Molecular Biology
- Record Identifier
- 9984025257102771
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