37. Sinha Roy A, Dzikovski B, Dolui D, Makhlynets O, Dutta A, Srivastava M. A Simulation Independent Analysis of Single- and Multi-Component cw ESR Spectra. Magnetochemistry 2023, 9(5), 112.

36. Bhattacharya S, Margheritis E, Takahashi K, Kulesha A, D’Souza A, Kim I, Yoon JH, Tame JRH, Volkov AN*, Makhlynets OV*, Korendovych IV*. NMR-guided directed evolution. Nature, 2022, 610:389-393.

35. Areetha D’Souza; Liam R. Marshall; Jennifer Yoon; Alona Kulesha; Dona I.U. Edirisinghe; Siddarth Chandrasekaran; Parth Rathee; Rajeev Prabhakar; Olga Makhlynets. Peptide hydrogel with self-healing and redox-responsive properties. Nano Convergence, 2022 9, 18.

34. Megha Jayachandran, Jennifer Yoon, Jacky Wu, Denis Cipurko, Joyce Quon, Olga Makhlynets. Mechanistic studies of the cofactor assembly in class Ib ribonucleotide reductases and protein affinity for Mn(II) and Fe(II). Metallomics, Volume 13, Issue 11, November 2021, mfab062.

33. Zsofia Lengyel-Zhand, Liam R Marshall, Maximilian Jung, Megha Jayachandran, Min-Chul Kim, Austin Kriews, Olga V Makhlynets, H Christopher Fry, Armin Geyer, Ivan V Korendovych. Covalent Linkage and Macrocylization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids. ChemBioChem, 2021, 22(3):585-591.

32. Areetha R D’SouzaMatthew R NecelisAlona KuleshaGregory A CaputoOlga V MakhlynetsBeneficial Impacts of Incorporating the Non-Natural Amino Acid Azulenyl-Alanine into the Trp-Rich Antimicrobial Peptide buCATHL4B. Biomolecules2021 Mar 12;11(3):421.

31. Olga Makhlynets*, Gregory Caputo* Characteristics and Therapeutic Applications of Antimicrobial Peptides. Biophysics Reviews, 2021, v. 2, 011301.

30. Alona Kulesha, Jennifer H.Yoon, Cara Chester, Areetha D’Souza, Christos Costeas, Olga V. Makhlynets.* Contributions of primary coordination ligands and importance of outer sphere interactions in UFsc, a de novo designed protein with high affinity for metal ions. Volume 212, November 2020, 111224.

29. Areetha D’Souza, Jennifer Yoon, Henry Beaman, Pallavi Gosavi, Zsofia Lengyel- Zhand, Alex Sternisha, Garrick Centola, Liam R. Marshall, Matthew D. Wehrman, Kelly M. Schultz, Mary Beth Monroe, Olga V. Makhlynets.* Nine-residue peptide self-assembles in the presence of silver to produce a self- healing, cytocompatible, antimicrobial hydrogel. ACS Applied Materials and Interfaces, 2020, 12, 17091–17099.

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, 25, 15252-15256.

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


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