Artificial metalloenzymes generally consist of a synthetic (organo)metallic catalyst incorporated into a protein. Asymmetric catalysis by such metalloenzymes could result by virtue of the chiral protein environment. Now, redox-sensitive anchoring enables reversible incorporation of an iridium catalyst for transfer hydrogenation.
This is a preview of subscription content, access via your institution
Relevant articles
Open Access articles citing this article.
-
Synthetic prodrug design enables biocatalytic activation in mice to elicit tumor growth suppression
Nature Communications Open Access 10 January 2022
Access options
Access Nature and 54 other Nature Portfolio journals
Get Nature+, our best-value online-access subscription
$29.99 / 30 days
cancel any time
Subscribe to this journal
Receive 12 digital issues and online access to articles
$119.00 per year
only $9.92 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
Change history
26 September 2018
In the version of this News & Views article originally published, in ref. 3, ‘https://doi.org/10.1038/s41929-018-124-3 was incorrect and should have read ‘https://doi.org/10.1038/s41929-018-124-3’. This has now been corrected in all versions.
References
Wilson, M. E. & Whitesides, G. M. J. Am. Chem. Soc. 100, 306–307 (1978).
Muñoz Robles, V. et al. J. Am. Chem. Soc. 136, 15676–15683 (2014).
Raines, D. J. et al. Nat. Catal. https://doi.org/10.1038/s41929-018-0124-3 (2018).
Schwizer, F. et al. J. Chem. Rev. 118, 142–231 (2018).
Blanco, V., Leigh, D. A. & Marcos, V. Chem. Soc. Rev. 44, 5341–5370 (2015).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Okuda, J. Reversible catalyst anchoring . Nat Catal 1, 639–640 (2018). https://doi.org/10.1038/s41929-018-0149-7
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41929-018-0149-7
This article is cited by
-
Synthetic prodrug design enables biocatalytic activation in mice to elicit tumor growth suppression
Nature Communications (2022)