In spite of the many functions of copper proteins within biology, those that contain a single copper ion can be divided into two classes, based in part on their spectroscopic properties. An artificial 'type 0' protein combines some properties of both, and may offer a route to stable catalytic processes.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Malkin, R. & Malmström, B. G. Adv. Enzymol. 33, 177–243 (1970).
Lancaster, K. M., DeBeer George, S., Yokoyama, K., Richards, J. H. & Gray, H. B. Nature Chem. 1, 711–715 10.1038/nchem.412(2009).
Gray, H. B., Malmström, B. G. & Williams, R. J. P. J. Biol. Inorg. Chem. 5, 551–559 (2000).
Solomon, E. I. Inorg. Chem. 45, 8012–8025 (2006).
Lu, Y., Yeung, N., Sieracki, N. & Marshall, N. M. Nature 460, 855–862 (2009).
Blanford, C. F., Foster, C. E., Heath, R. S. & Armstrong, F. A. Faraday Discuss. 140, 319–335 (2008).
Mizoguchi, T. J., Di Bilio, A. J., Gray, H. B. & Richards, J. H. J. Am. Chem. Soc. 114, 10076–10078 (1992).
Lancaster, K. M., Yokoyama, K., Richards, J. H., Winkler, J. R. & Gray, H. B. Inorg. Chem. 48, 1278–1280 (2009).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Rosenzweig, A. Zeroing in on a new copper site. Nature Chem 1, 684–685 (2009). https://doi.org/10.1038/nchem.456
Issue Date:
DOI: https://doi.org/10.1038/nchem.456
