The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Artificial Metalloenzymes and Metallopeptide Catalysts for Organic Synthesis
Abstract
Transition metal catalysts and enzymes possess unique and often complementary properties that have made them important tools for chemical synthesis. The potential practical benefits of catalysts that combine these properties and a desire to understand how the structure and reactivity of metal and peptide components affect each other have driven researchers to create hybrid metal–peptide catalysts since the 1970s. The hybrid catalysts developed to date possess unique compositions of matter at the inorganic/biological interface that often pose significant challenges from design, synthesis, and characterization perspectives. Despite these obstacles, researchers have developed systems in which secondary coordination sphere effects impart selectivity to metal catalysts, accelerate chemical reactions, and are systematically optimized via directed evolution. This perspective outlines fundamental principles, key developments, and future prospects for the design, preparation, and application of peptide- and protein-based hybrid catalysts for organic transformations.
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Cites
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
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Opportunities for merging chemical and biological synthesis
Wallace, S., & Balskus, E. P. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.03.006 · Cited by 86
“This approach, which was originally pioneered by Whitesides [32], has been applied to a variety of protein scaffolds and transition metal complexes [33,34].”
Metadata
- Authors
- Lewis, J. C.
- Venue
- ACS Catalysis
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-11-18
- Volume
- 3
- Issue
- 12
- Pages
- 2954-2975
- ISSN
- 2155-5435 (ISSN-L)
- OpenAlex
- W1978964903
- Cited by
- 270
- References
- 1
- FWCI
- 12.10
- Type
- journal article
- Language
- en
- Open access
- closed
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