The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Artificial Metalloenzymes: Challenges and Opportunities
Open accessAbstract
Abstract Artificial metalloenzymes (ArMs) result from the incorporation of an abiotic metal cofactor within a protein scaffold. From the earliest techniques of transition metals adsorbed on silk fibers, the field of ArMs has expanded dramatically over the past 60 years to encompass a range of reaction classes and inspired approaches: Assembly of the ArMs has taken multiple forms with both covalent and supramolecular anchoring strategies, while the scaffolds have been intuitively selected and evolved, repurposed, or designed in silico. Herein, we discuss some of the most prominent recent examples of ArMs to highlight the challenges and opportunities presented by the field.
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Cites
Comprehensive asymmetric catalysis
Jacobsen, E. N., Pfaltz, A., & 山本, 尚. (1999) · Springer eBooks · Cited by 3,786
The Moderately Efficient Enzyme: Evolutionary and Physicochemical Trends Shaping Enzyme Parameters
Bar-Even, A., Noor, E., Savir, Y., Liebermeister, W., Davidi, D., Tawfik, D. S., & Milo, R. (2011) · Biochemistry · doi:10.1021/bi2002289 · Cited by 1,050
Cellular Incorporation of Unnatural Amino Acids and Bioorthogonal Labeling of Proteins
Lang, K., & Chin, J. W. (2014) · Chemical Reviews · doi:10.1021/cr400355w · Cited by 1,035
Artificial Metalloenzymes: Reaction Scope and Optimization Strategies
Schwizer, F., Okamoto, Y., Heinisch, T., Gu, Y., Pellizzoni, M. M., Lebrun, V., Reuter, R., Köhler, V., Lewis, J. C., & Ward, T. R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00014 · Cited by 831
Self-citationBiotinylated Rh(III) Complexes in Engineered Streptavidin for Accelerated Asymmetric C–H Activation
Hyster, T. K., Knörr, L., Ward, T. R., & Rovis, T. (2012) · Science · doi:10.1126/science.1226132 · Cited by 814
Self-citationKrishnamurthy, V. M., Kaufman, G. K., Urbach, A. R., Gitlin, I., Gudiksen, K. L., Weibel, D. B., & Whitesides, G. M. (2008) · Chemical Reviews · doi:10.1021/cr050262p · Cited by 761
Wilson, M. E., & Whitesides, G. M. (1978) · Journal of the American Chemical Society · doi:10.1021/ja00469a064 · Cited by 541
Directed evolution of artificial metalloenzymes for in vivo metathesis
Jeschek, M., Reuter, R., Heinisch, T., Trindler, C., Klehr, J., Panke, S., & Ward, T. R. (2016) · Nature · doi:10.1038/nature19114 · Cited by 456
Self-citationAbiological catalysis by artificial haem proteins containing noble metals in place of iron
Key, H. M., Dydio, P., Clark, D. S., & Hartwig, J. F. (2016) · Nature · doi:10.1038/nature17968 · Cited by 442
An artificial metalloenzyme with the kinetics of native enzymes
Dydio, P., Key, H. M., Nazarenko, A., Rha, J. Y.-E., Seyedkazemi, V., Clark, D. S., & Hartwig, J. F. (2016) · Science · doi:10.1126/science.aah4427 · Cited by 384
Cited by
Chemical modifications of proteins and their applications in metalloenzyme studies
Naowarojna, N., Cheng, R., Lopez, J., Wong, C., Qiao, L., & Liu, P. (2021) · Synthetic and Systems Biotechnology · doi:10.1016/j.synbio.2021.01.001 · Cited by 52
Metadata
- Authors
- Davis, H. J., & Ward, T. R.
- Venue
- ACS Central Science
- Publisher
- American Chemical Society (ACS)
- Published
- 2019-07-16
- Volume
- 5
- Issue
- 7
- Pages
- 1120-1136
- ISSN
- 2374-7943 (ISSN-L)
- 2374-7951
- OpenAlex
- W2961566029
- Cited by
- 283
- References
- 59
- FWCI
- 10.00
- Type
- journal article
- Language
- en
- Open access
- diamond
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
