This work was supported by the BBSRC through Grant #SBD07575 and an Advanced Fellowship to P.D.B. We thank Alan Fersht for support and access to facilities, and Shankar Balasubramanian for critical reading of the manuscript.
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Communication
Controlling Self-Assembly by Linking Protein Folding, DNA Binding, and the Redox Chemistry of Heme†
Article first published online: 15 SEP 2005
DOI: 10.1002/anie.200463035
Copyright © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Jones, D. D. and Barker, P. D. (2005), Controlling Self-Assembly by Linking Protein Folding, DNA Binding, and the Redox Chemistry of Heme. Angew. Chem. Int. Ed., 44: 6337–6341. doi: 10.1002/anie.200463035
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Publication History
- Issue published online: 30 SEP 2005
- Article first published online: 15 SEP 2005
- Manuscript Revised: 13 JUL 2005
- Manuscript Received: 22 DEC 2004
Keywords:
- cytochromes;
- DNA binding;
- heme;
- protein folding;
- self-assembly
Heme recognizes genes: As a step towards the electronic control of reading DNA code at a molecular level, heme and DNA recognition can be linked through protein folding (see picture). Through the conversion of an engineered DNA-binding cytochrome into a heterodimer, the sequence-specific DNA recognition can be controlled by heme recognition and the oxidation state of the iron center.