Artificial metalloenzyme

An Artificial Metalloenzyme (ArM) is a designer metalloprotein, not found in nature, which can catalyze desired chemical reactions.[1][2] Despite fitting into classical enzyme categories, ArMs also have potential in new-to-nature chemical reactivity like catalysing Suzuki coupling,[3] Metathesis[4] etc., which were never reported among natural enzymatic reactions.

Pd-silk fibroin complex catalyzed asymmetric hydrogenation

ArMs have two main components: a protein scaffold and an artificial catalytic moiety, which, in this case, features a metal center. This class of designer biocatalysts is unique because of the potential to improve the catalytic performance through chemogenetic optimization, a parallel improvement of both the direct metal surrounding (first coordination sphere) and the protein scaffold (second coordination sphere).The second coordination sphere (protein scaffold) is easily evolvable and, in the case of ArMs, responsible for very high (stereo)selectivity.[5] With the progress in organometallic synthesis and protein engineering, more and more new kind of design of ArMs were developed, showing promising future in both academia and industrial aspects.[6]

In 2018, one-half of the Nobel Prize in Chemistry was awarded to Frances H. Arnold "for the directed evolution of enzymes", who elegantly evolved artificial metalloenzymes to realize efficient and highly selective new-to-nature chemical reactions in vitro and in vivo.

  1. ^ Morra S, Pordea A (October 2018). "Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase". Chemical Science. 9 (38). Royal Society of Chemistry: 7447–7454. doi:10.1039/C8SC02371A. PMC 6180310. PMID 30319745.
  2. ^ Leurs M, Dorn B, Wilhelm S, Manisegaran M, Tiller JC (July 2018). "Multicore Artificial Metalloenzymes Derived from Acylated Proteins as Catalysts for the Enantioselective Dihydroxylation and Epoxidation of Styrene Derivatives". Chemistry: A European Journal. 24 (42): 10859–10867. doi:10.1002/chem.201802185. PMID 29808506.
  3. ^ Chatterjee A, Mallin H, Klehr J, Vallapurackal J, Finke AD, Vera L, et al. (January 2016). "An enantioselective artificial Suzukiase based on the biotin-streptavidin technology". Chemical Science. 7 (1): 673–677. doi:10.1039/C5SC03116H. PMC 5953008. PMID 29896353.
  4. ^ Jeschek M, Reuter R, Heinisch T, Trindler C, Klehr J, Panke S, et al. (September 2016). "Directed evolution of artificial metalloenzymes for in vivo metathesis" (PDF). Nature. 537 (7622): 661–665. Bibcode:2016Natur.537..661J. doi:10.1038/nature19114. PMID 27571282. S2CID 205250261.
  5. ^ Cite error: The named reference :5 was invoked but never defined (see the help page).
  6. ^ Schwizer F, Okamoto Y, Heinisch T, Gu Y, Pellizzoni MM, Lebrun V, et al. (January 2018). "Artificial Metalloenzymes: Reaction Scope and Optimization Strategies" (PDF). Chemical Reviews. 118 (1): 142–231. doi:10.1021/acs.chemrev.7b00014. PMID 28714313.