28. Makhlynets OV, Korendovych IV. 2019, Nature Catalysis, 2, 949-950
Sharable link of the News and Views paper:
“A single amino acid enzyme” has gained much interest and was already shared over 300 times on Twitter:
27. Yoon JH, Kulesha AV, Lengyel‐Zhand Z, Volkov AN, Rempillo JJL, D’Souza A, Costeas C, Chester C, Caselle ER, Makhlynets OV*. Uno Ferro, a de novo designed protein, binds transition metals with high affinity and stabilizes semiquinone radical anion. Chem. Eur. J., 2019, accepted paper
26. Caselle EA+, Yoon JH+, Bhattacharya S, Rempillo JJL, Lengyel Z, D’Souza A, Moroz YS, Tolbert PL, Volkov AN, Forconi M, Castañeda CA, Makhlynets OV*, and Korendovych IV*. Kemp eliminases of the AlleyCat family possess high substrate selectivity. ChemCatChem, 2019, 1425-1430.
The Front Cover picture shows that AlleyCat2, a member of the AlleyCat family of allosterically regulated Kemp eliminases, is capable of binding leflunomide, an immunosuppressant drug, and converting it into teriflunomide, its active form, with remarkable efficiency. In their Communication, E. A. Caselle, J. H. Yoon et al. show that small libraries of designed catalysts provide fertile ground for discovering new reactivities. AlleyCat2 relies on a high pKa of the active base and proper positioning of the substrate in the hydrophobic cleft of the enzyme to promote catalysis. This work also demonstrates that using pH rate profiles to determine the pKa of the active residue can be quite misleading and NMR studies that can probe specific atoms directly provide invaluable mechanistic information.
25. Gosavi PM, Jayachandran M, Rempillo JJL, Zozulia O, Makhlynets OV, Korendovych IV. A designed enzyme promotes selective post‐translational acylation. ChemBioChem, 2018, May 13. Has been selected as a cover article.
The cover feature picture shows how a computationally designed allosterically regulated esterase CaM M144H, a derivative of AlleyCatE, can recognize and specifically post‐translationally modify helical domains (highlighted in green) in calmodulin‐binding proteins with an unnatural tag providing structural and functional insight into protein–protein interactions.
We would like to thank Katelyn Leets from the Chisholm lab for helping us to photograph her cat Lola!
|24. Lengyel Z, Rufo CM, Moroz YS, Makhlynets OV, Korendovych IV. Copper-containing catalytic amyloids promote phosphoester hydrolysis and tandem reactions. ACS Catal, 2018, 8, 59–62. Has been selected as a cover article for the first issue of 2018.
|23. Makhlynets OV*, Korendovych IV*. Finding a silver bullet in a stack of proteins. Biochemistry. 2017, 56, 6627–6628. PMID: 29232102
|22. Lee M, Wang T, Makhlynets OV, Wu Y, Polizzi NF, Wu H, Gosavi PM, Stöhr J, Korendovych IV, DeGrado WF, Hong M. Zinc-binding structure of a catalytic amyloid from solid-state NMR. Proc Natl Acad Sci USA. 2017, 114(24), 6191-6196. PMID:28566494
|21. Hiebler K, Lengyel Z, Castañeda CA, Makhlynets OV. Functional tuning of the catalytic residue pKa in a de novo designed esterase. Proteins 2017, 9, 1656-1665. PMID: 28544090
|20. Takacs M, Makhlynets OV, Tolbert PL, Korendovych IV. Secretion of functional formate dehydrogenase in Pichia pastoris. Protein Eng Des Sel. 2017, 30(3), 381-386. PMID: 28201611|
|19. Sternisha AC, Makhlynets OV. Catalytic amyloid fibrils that bind copper to activate oxygen. Methods Mol Biol. 2017, 1596, 59-68. PMID: 28293880
|18. Makhlynets O.V., Korendovych I.V. Minimalist Design of Allosterically Regulated Protein Catalysts. Methods Enzymol. 2016, 580, 191-202. PMID: 27586334|
|17. Makhlynets O.V., Korendovych I.V. Enzyme design: Functional Frankensteins. Nat. Chem. 2016, Aug 24, 8(9), 823-4. PMID: 27554407
|16. Makhlynets O.V., Gosavi P.M., Korendovych I.V. Short Self-assembling Peptides are Able to Bind to Copper and Activate Oxygen. Angew. Chem. Int. Ed. Engl. 2016, Jul 25, 55(31), 9017-20. PMID: 27276534
|15. Maeda Y., Makhlynets O.V., Matsui H., Korendovych I.V. Design of Catalytic Peptides and Proteins Through Rational and Combinatorial Approaches. Annu. Rev. Biomed. Eng. 2016, Jul 11(18), 311-28. PMID: 27022702|
|14. Moroz Y.S., Dunston T.T., Makhlynets O.V., Moroz O.V., Wu Y., Yoon J.H., Olsen A.B., McLaughlin J.M., Mack K.L., Gosavi P.M., van Nuland N.A.J., Korendovych I.V. New Tricks for Old Proteins: Single Mutations in a Nonenzymatic Protein Give Rise to Various Enzymatic Activities. Journal of the American Chemical Society. 2015, 137(47), 14905-11. PMCID: PMID: 26555770|
|13. Makhlynets, O.V., Raymond, E.A., and Korendovych, I.V.* Design of Allosterically Regulated Protein Catalysts. Biochemistry, 2015, 54, 1444-1456. Highlighted on the Biochemistry website.|
|12. Makhlynets, O.V., Korendovych I.V. De novo design of catalytically amplified sensors for small molecules. Biomolecules, 2014, 4(2), 402-418. PMID: 24970222|
POSTDOCTORAL AND GRADUATE WORK
|11. Makhlynets, O.V., Boal, A.K., Rhodes, D.V., Kitten, T., Rosenzweig, A.C, Stubbe, J. Streptococcus sanguinis class Ib ribonucleotide reductase: high activity with both iron and manganese cofactors and structural insights. J. Biol. Chem. 2014, 289(9), 6259-6272. PMID: 24381172|
|10. Rhodes, D.V., Crump, K.E., Makhlynets, O.V., Snyder, M., Ge, X., Xu, P., Stubbe J., and Kitten, T. Genetic characterization and role in virulence of the ribonucleotide reductases of Streptococcus sanguinis. J. Biol. Chem. 2014, 289(9), 6273-6287. Has been selected as a paper of the week (top 2% of all papers submitted to the journal). PMID: 24381171|
|9. Makhlynets, O.V.; Oloo, W.; Moroz, Y.S.; Belaya, I.G.; Palluccio, T.D.; Filatov, A.S.; Müller, P.; Cranswick, M.A.; Que, L., Jr. and Rybak-Akimova, E.V. H2O2 activation with biomimetic non-haem iron complexes and AcOH: connecting the g = 2.7 EPR signal with a visible chromophore. Chem. Commun., 2014, 50, 645-648. Has been selected as a cover article of the issue (Issue 6, January 21, 2014). PMID: 24292104
|8. Mykhalyova, E.A.; Makhlynets, O.V.; Palluccio, T.D.; Filatov, A.S.; Rybak-Akimova, E.V. New efficient iron catalyst for olefin epoxidation with hydrogen peroxide. Chem. Commun., 2012, 48, 687-689. PMID: 22134336|
|7. Kryatova, M.S.; Makhlynets, O.V.; Nazarenko, A.Y. Nickel(II) complexes with tetradentate N-4 ligands: synthesis, structure, electrochemistry and thermochromism in solution. Inorg. Chim. Acta 2012, 387, 74-80. doi:10.1016/j.ica.2011.12.054|
|6. Huang, D.; Makhlynets, O.V.; Tan, L.L.; Lee, S.C.; Rybak-Akimova, E.V.; Holm, R.H. Fast carbon dioxide fixation by 2,6-pyridinedicarboxamidato-nickel(II)-hydroxide complexes: influence of changes in reactive site environment on reaction rates. Inorg. Chem., 2011, 50(20), 10070-10081. PMID: 21905646|
|5. Makhlynets, O.V.; Rybak-Akimova, E.V. Aromatic hydroxylation at a non-heme iron center: observed intermediates and insights into the nature of the active species. Chem. Eur. J., 2010, 16(47), 13995-14006 Has been selected as a cover article of the issue (Issue 47, December 17, 2010). PMID: 21117047
|4. Huang, D.; Makhlynets, O.V.; Tan, L.L.; Rybak-Akimova, E.V.; Lee, S.C.; Holm, R.H. Extremely rapid carbon dioxide fixation: kinetics and mechanistic analysis. Proc. Natl. Acad. Sci. USA, 2011, 108(4), 1222-1227. PMID: 21220298|
|3. Makhlynets, O.V.; Das, P.; Taktak, S.; Flook, M.; Mas-Ballesté, R.; Rybak-Akimova, E.V.; Que, L., Jr. Iron-promoted ortho– and/or ipso-hydroxylation of benzoic acids with H2O2. Chem. Eur. J., 2009, 15(47), 13171-13180. PMID: 19876966|
|2. Korendovych, I.V.; Cho, M.; Makhlynets, O.V.; Butler, P.L.; Staples, R.J.; Rybak-Akimova, E.V. Anion and carboxylic acid binding to monotopic and ditopic amidopyridine macrocycles. J. Org. Chem., 2008, 73(13), 4771-4782. Has been selected as a cover article of the issue (Issue 13, July 4, 2008). PMID: 18396906
|1. Korendovych, I.V.; Makhlynets, O.V.; Buzak, S.K.; Flook, M.M.; Kryatov, S.V.; Haas, T.E.; Rybak-Akimova, E.V. (1R,2R)-(+)-4,4′-Di-tert-butyl-2,2′-[1,2-diphenylethane-1,2-diylbis(nitrilomethylidyne)]diphenol. Acta Cryst., Section E, 2006, E62(4), o1240-o1242. doi:10.1107/S1600536806007136|