The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Hydrolytic catalysis and structural stabilization in a designed metalloprotein
Open accessAbstract
Metal ions are an important part of many natural proteins, providing structural, catalytic and electron transfer functions. Reproducing these functions in a designed protein is the ultimate challenge to our understanding of them. Here, we present an artificial metallohydrolase, which has been shown by X-ray crystallography to contain two different metal ions – a Zn(II) ion which is important for catalytic activity and a Hg(II) ion which provides structural stability. This metallohydrolase displays catalytic activity that compares well with several characteristic reactions of natural enzymes. It catalyses p-nitrophenyl acetate hydrolysis (pNPA) to within ~100-fold of the efficiency of human carbonic anhydrase (CA)II and is at least 550-fold better than comparable synthetic complexes. Similarly, CO2 hydration occurs with an efficiency within ~500-fold of CAII. While histidine residues in the absence of Zn(II) exhibit pNPA hydrolysis, miniscule apopeptide activity is observed for CO2 hydration. The kinetic and structural analysis of this first de novo designed hydrolytic metalloenzyme uncovers necessary design features for future metalloenzymes containing one or more metals.
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Cites
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A zinc(II) complex of 1,5,9-triazacyclododecane ([12]aneN3) as a model for carbonic anhydrase
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De novo design of catalytic proteins
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Designing artificial enzymes by intuition and computation
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Cited by
Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO 2 Fixation
Appel, A. M., Bercaw, J. E., Bocarsly, A. B., Dobbek, H., DuBois, D. L., Dupuis, M., Ferry, J. G., Fujita, E., Hille, R., Kenis, P. J. A., et al. (2013) · Chemical Reviews · doi:10.1021/cr300463y · Cited by 2,193
Brunk, E., & Rothlisberger, U. (2015) · Chemical Reviews · doi:10.1021/cr500628b · Cited by 494
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Self-citationComputational design of serine hydrolases
Lauko, A., Pellock, S. J., Sumida, K. H., Anishchenko, I., Juergens, D., Ahern, W., Jeung, J., Shida, A. F., Hunt, A., Kalvet, I., et al. (2025) · Science · doi:10.1126/science.adu2454 · Cited by 235
Carbon sequestration via carbonic anhydrase facilitated magnesium carbonate precipitation
Power, I. M., Harrison, A. L., Dipple, G. M., & Southam, G. (2013) · International Journal of Greenhouse Gas Control · doi:10.1016/j.ijggc.2013.03.011 · Cited by 99
Metadata
- Authors
- Zastrow, M. L., Peacock, A. F. A., Stuckey, J. A., & Pecoraro, V. L.
- Venue
- Nature Chemistry
- Published
- 2011-11-27
- Volume
- 4
- Issue
- 2
- Pages
- 118-123
- ISSN
- 1755-4330 (ISSN-L)
- 1755-4349
- OpenAlex
- W2093448565
- Cited by
- 355
- References
- 24
- FWCI
- 8.82
- Type
- journal article
- Language
- en
- Open access
- green
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- Zastrow, M. L., Peacock, A. F. A., Stuckey, J. A., & Pecoraro, V. L. (2012). Hydrolytic catalysis and structural stabilization in a designed metalloprotein. Nature Chemistry. https://doi.org/10.1038/nchem.1201
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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