
“Highly Sensitive Detection of Tyrosine and Neurotransmitters by Stereoselective Biosynthesis and Photochemically Induced Dynamic Nuclear Polarization”
Shapla, U. M.; Smith, J. L.; Halder, A.; Thompson, L.; Buller, A. R.; Cavagnero, S. J. Am. Chem. Soc. 2025.

“Active site diversification of a non-canonical amino acid
decarboxylase by merging substrate multiplexed screening
with computationally guided recombination”
McDonald, A. D.; Ellis, J. M.; Steger-Wilson, L.; Campbell, M. E.; Buller, A. R. Protein Science 2025, 34 (11), e70356.

“Enhanced Stereochemical Analysis of β-Diastereomeric Amino Acids with Variants of Marfey’s Reagent”
Studinski, C. I.; Powers, M. K.; Martin, B. K.; Mosconi, A. L.; Abraham, J. A.; Koss, K. R.; Bruffy, S. K.; Campbell, M. E.; Buller, A. R.; Willoughby, P. H. ACS Omega 2025, 10 (43), 51677–51685.

“Biocatalytic synthesis of β-hydroxy tryptophan regioisomers”
Bruffy, S. K.; Samuel, H.; Weilbaker, H. A.; Buller, A. R. Org. Biomol. Chem. 2025, 23 (43), 9857–9861.

“Cobalt-Substituted Hemoprotein Expression”
Rodemeier, M. E.; Holsinger, O. P.; Buller, A. R. In Methods in Enzymology; Academic Press, 2025.
https://doi.org/10.1016/bs.mie.2025.06.031

“Promiscuity Guided Evolution of Decarboxylative Aldolases for
Synthesis of Tertiary γ-Hydroxy Amino Acids”
M. E. Campbell, A. R. Ohler, M. J. McGill, A. R. Buller, Angew. Chem. Int. Ed. 2025, 64, e202422109.

“Chemoenzymatic Cascade Synthesis of Metal-Chelating α-Amino Acids”
S. H. Young, J. S. Andon, J. Lim, M. C. Franke, D. J. Weix, T. Wang, A. R. Buller. ChemCatChem 2025, e202401958.

“Substrate-Multiplexed Assessment of Aromatic Prenyltransferase Activity”
, , , ChemBioChem 2024, e202400680.

“Biocatalytic asymmetric aldol addition into unactivated ketones”
Bruffy, S.K., Meza, A., Soler, J. et al. Nat. Chem. (2024).
“Elucidation of the Stereochemical Mechanism of Cystathionine γ-Lyase Reveals How Substrate Specificity Constrains Catalysis”
Anna Zmich, Lydia J. Perkins, Craig Bingman, and Andrew R. Buller. ACS Catalysis 2024 14 (15), 11196-11204

“Molecular Determinants of Efficient Cobalt-Substituted Hemoprotein in E. coli“
Weaver, B.R.; Perkins, L.J.; Fernandez Candelaria, F.O.; Burstyn, J.N.; Buller, A.R. ACS Synth. Biol. 2023.

“Engineered Biocatalytic Synthesis of β-N-Substituted-⍺-Amino Acids”
Villalona, J.; Higgins, P.M.; Buller, A.R. Angewandte Chemie. 2023, e202311
https://onlinelibrary.wiley.com/doi/full/10.1002/anie.202311189

“Multiplexed Assessment of Promiscuous Non-Canonical Amino Acid Synthase Activity in a Pyridoxal Phosphate-Dependent Protein Family”
Zmich, A.; Perkins, L.J.; Bingman, C.; Acheson, J.F.; Buller, A.R. ACS Catal. 2023, 11644–11655
https://pubs.acs.org/doi/10.1021/acscatal.3c02498

“Engineering Enzyme Substrate Scope Complementarity for Promiscuous Cascade Synthesis of 1,2-Amino Alcohols”
McDonald, A.D.; Bruffy, S.K.; Kasat, A.T.; Buller, A.R. Angewandte Chemie. 2022, e202212637
https://onlinelibrary.wiley.com/doi/full/10.1002/anie.202212637

“Substrate multiplexed protein engineering facilitates promiscuous biocatalytic synthesis”
McDonald, A.D.; Higgins, P.M.; Buller, A.R. Nat Comm. 2022, 13, 5242
https://www.nature.com/articles/s41467-022-32789-w
Previously posted on ChemRxiv https://chemrxiv.org/engage/chemrxiv/article-details/618da1579960f3d941a8bed9

“Efficient Chemoenzymatic Synthesis of α-Aryl Aldehydes as Intermediates in C–C Bond Forming Biocatalytic Cascades”
Meza, A.; Campbell, M. E.; Zmich, A.; Thein, S. A.; Grieger, A. M.; McGill, M. J.; Willoughby, P. H.; Buller, A. R. ACS Catal. 2022, 12 (17), 10700–10710.

“Investigation of β-substitution activity of O-acetylserine sulfhydrolase from Citrullus vulgaris”
Smith, J. L.; Harrison, I. M.; Bingman, C. A.; Buller, A. R. ChemBioChem 2022, 23 (14), e202200157.
https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202200157

“Site-selective deuteration of amino acids through dual-protein catalysis”
Doyon, T.J.; Buller, A.R. J. Am. Chem. Soc. 2022. 144, 16, 7327-7336.

“Biocatalytic synthesis of non-standard amino acids by a decarboxylative aldol reaction”
Ellis, J.M.; Campbell, M.E.; Kumar, P.; Geunes, E.P.; Bingman, C.A.; Buller, A.R. Nat Catal.5, 136–143 (2022)

“Scalable and selective β-hydroxy-α-amino acid synthesis catalyzed by promiscuous L-threonine transaldolase ObiH”
Doyon, T.J.; Kumar, P.; Thein, S.; Kim, M.; Stitgen, A.; Grieger, A.M.; Madigan, C.; Willoughby, P.H.; Buller, A.R. ChemBioChem. 2021

“De novo biosynthesis of a nonnatural cobalt porphyrin cofactor in E. coli and incorporation into hemoproteins”
Perkins, L.J.; Weaver, B.R.; Buller, A.R.; Burstyn, J.N. PNAS. 2021

“L-Threonine transaldolase activity is enabled by a persistent catalytic intermediate”
Kumar, P.; Meza, A.; Ellis, J. M.; Carlson, G. A.; Bingman, C. A.; Buller, A. R. ACS Chemical Biology. 2020

“Modular control of L-tryptophan isotopic substitution via an efficient biosynthetic cascade”
Thompson, C.; McDonald, A.; Yang, H.; Cavagnero, S.; Buller, A. R. Organic & Biomolecular Chemistry. 2020

“Facile in vitro biocatalytic production of diverse tryptamines”
McDonald, A.; Perkins, L.; Buller, A. R. ChemBioChem 2019.
Other publications:
2025
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Brousseau, M.; Dash, T.; Rourke, M. J.; Kurauskas, V.; Tonelli, M.; Hibbs, K. M.; Buller, A. R.; Marty, M. T.; Henzler-Wildman, K. A. 18-Crown-6-Ether Utilizes Distinct Allosteric Interactions to Uncouple Transport by the Multidrug Efflux Pump EmrE. Biochemistry 2025, 64 (18), 3956–3970. https://doi.org/10.1021/acs.biochem.5c00348.
2024
- Sanders, K. M.; Bruffy, S. K.; Buller, A. R.; Petříček, V.; Guzei, I. A. Occupational Modulation in the (3+1)-Dimensional Incommensurate Structure of (2S,3S)-2-Amino-3-Hydroxy-3-Methyl-4-Phenoxybutanoic Acid Dihydrate. Acta Cryst C 2024, 80 (9), 523–533. https://doi.org/10.1107/S2053229624007009.
2020
- Beasley, M., Lumley, M., Janicki, T., Fernandez, R., Manger, L., Tucholski, T., Thomas, N., Whitmire, L., Lawson, A., Buller, A.R. J. Chem. Educ. 2020, 97, 3, 643–650. Student-Led Climate Assessment Promotes a Healthier Graduate School Environment. https://doi.org/10.1021/acs.jchemed.9b00611
2019
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Patel KD, d’Andrea FB, Gaudelli NM, Buller AR, Townsend CA, Gulick AM. Nat Commun. 2019 Aug 27;10(1):3868. Structure of a bound peptide phosphonate reveals the mechanism of nocardicin bifunctional thioesterase epimerase-hydrolase half-reactions. doi.org/10.1038/s41467-019-11740-6
2018
- Kan, S. B. J.; Garcia-Borràs, M.; Lewis, R. D.; Houk, K. N.; Chalkley, M. J.; Buller, A. R.; Arnold, F. H. Proc. Natl. Acad. Sci. 2018, 115 (28), 7308. doi.org/10.1073/pnas.1807027115
- . 2018. Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble. Journal of the American Chemical Society. doi.org/10.1021/jacs.8b03490
- . 2018. Engineered Biosynthesis of beta-Alkyl Tryptophan Analogues. Angewandte Chemie-International Edition. 57:14764-14768. doi.org/10.1002/anie.201807998
2017
- . 2017. Enantioselective, intermolecular benzylic C-H amination catalysed by an engineered iron-haem enzyme. Nature Chemistry. 9:629-634. doi.org/10.1038/nchem.2783
2016
- . 2016. Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases. Protein ScienceProtein Science. 25:1241-1248. doi.org/10.1002/pro.2852
- . 2016. A Panel of TrpB Biocatalysts Derived from Tryptophan Synthase through the Transfer of Mutations that Mimic Allosteric Activation. Angewandte Chemie-International Edition. 55:11577-11581. doi.org/10.1002/anie.201606242
- . 2016. Synthesis of beta-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase. Journal of the American Chemical Society. 138:8388-8391. doi.org/10.1021/jacs.6b04836
- . 2016. Tryptophan Synthase Uses an Atypical Mechanism To Achieve Substrate Specificity. Biochemistry. 55:7043-7046. doi.org/10.1021/acs.biochem.6b01127
2015
- . 2015. Cofactor specificity motifs and the induced fit mechanism in class I ketol-acid reductoisomerases. Biochemical Journal. 468:475-484. doi.org/10.1042/bj20150183
- . 2015. Consecutive radical S-adenosylmethionine methylations form the ethyl side chain in thienamycin biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 112:10354-10358. doi.org/10.1073/pnas.1508615112
- . 2015. Directed evolution of the tryptophan synthase beta-subunit for stand-alone function recapitulates allosteric activation. Proceedings of the National Academy of Sciences of the United States of America. 112:14599-14604. doi.org/10.1073/pnas.1516401112
- . 2015. Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450. Journal of the American Chemical Society. 137:13861-13865. doi.org/10.1021/jacs.5b07107
2014
- . 2014. Enzyme-Controlled Nitrogen-Atom Transfer Enables Regiodivergent C-H Amination. Journal of the American Chemical Society. 136:15505-15508. doi.org/10.1021/ja509308v
- . 2014. Exploring the Role of Conformational Heterogeneity in cis-Autoproteolytic Activation of ThnT. Biochemistry. 53:4273-4281. doi.org/10.1021/bi500385d
2013
- . 2013. Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad. Proceedings of the National Academy of Sciences of the United States of America. 110:E653-E661. doi.org/10.1073/pnas.1221050110
2012
- . 2012. Autoproteolytic Activation of ThnT Results in Structural Reorganization Necessary for Substrate Binding and Catalysis. Journal of Molecular Biology. 422:508-518. doi.org/10.1016/j.jmb.2012.06.012
- . 2012. Insights into cis-autoproteolysis reveal a reactive state formed through conformational rearrangement. Proceedings of the National Academy of Sciences of the United States of America. 109:2308-2313. doi.org/10.1073/pnas.1113633109
2008
- . 2008. A Homozygous Mutation in Human PRICKLE1 Causes an Autosomal-Recessive Progressive Myoclonus Epilepsy-Ataxia Syndrome. American Journal of Human Genetics. 83:572-581. doi.org/10.1016/j.ajhg.2008.10.003
