Johnsen, N. K., Marcher, D. M. W., Nielsen, M. B.
, Zhang, Y., Guo, Z. & Eser, B. E. (2025).
A Thermostable Fatty Acid Hydratase from Marinitoga Piezophila with Low Temperature Optimum and Broad Product Scope.
ChemBioChem,
26(17), Article e202500081.
https://doi.org/10.1002/cbic.202500081
Johnsen, N. K., Chaiyasarn, S.
, Guo, Z., Han, J.
& Eser, B. E. (2025).
Cobalamin-Dependent Aryl Methyl Ether O-Demethylases: Promising Enzymes for Biocatalytic Applications from Lignin Valorization to Organic Synthesis.
ChemCatChem,
17(21), 1-19. Article e00877.
https://doi.org/10.1002/cctc.202500877
Li, Z., Zhang, Y., Balle, T.
, Eser, B. E., Fang, Y.
& Guo, Z. (2025).
Preparation of Cello-Oligosaccharides by Precise-Controlled Enzymatic Depolymerization and Its Amphiphilic Functionalization for High-Oil Load Emulsification.
Journal of Agricultural and Food Chemistry,
73(2), 1458–1467.
https://doi.org/10.1021/acs.jafc.4c08886
Plesner, T. J., Wang, F., Ouyang, Y., Khazaee, Z., Zhou, P., Zhang, M.
, Eser, B. E., Zhang, Y. & Guo, Z. (2025).
Cooperative action from Cu-centered MOF and a laccase for enhanced decolorization of synthetic dyes.
Biochemical Engineering Journal,
221, 1-10. Article 109807.
https://doi.org/10.1016/j.bej.2025.109807
Benfeldt, F. V., Wang, F., Bredahl, N., Gao, R.
, Guo, Z. & Eser, B. E. (2024).
A Highly Efficient Ferulic Acid Decarboxylase from Capronia coronata: Characterization and Biocatalytic Applications. (pp. xxx-xxx). ChemRxiv
https://doi.org/10.26434/chemrxiv-2024-0npph-v2
Chanquia, S. N., Bittner, J. P.
, Santner, P., Szabó, L. K.
, Madsen, J. S., Øhlenschlæger, M. L., Sarvari, A. G.
, Merrild, A. H., Fo̷nss, K. G., Jaron, D., Lutz, L.
, Kara, S. & Eser, B. E. (2024).
Active-Site Mutagenesis of Fatty Acid Photodecarboxylase: Experimental and Computational Insight into Substrate Chain-Length Specificity.
ACS Catalysis,
14(21), 15837-15849.
https://doi.org/10.1021/acscatal.4c02970
Kim, H., Mi, H. T. N., Ahn, J. H., Lee, J. S.
, Eser, B. E., Choi, J. & Han, J. (2024).
Glycoside-metabolizing oxidoreductase D3dgpA from human gut bacterium.
Frontiers in Bioengineering and Biotechnology,
12, Article 1413854.
https://doi.org/10.3389/fbioe.2024.1413854Mi, H. T. N., Kim, H., Lee, J. S.
, Eser, B. E. & Han, J. (2024).
Flavonoids Biotransformation by Human Gut Bacterium Dorea sp. MRG-IFC3 Cell-Free Extract.
Journal of Microbiology and Biotechnology,
34(6), 1270-1275.
https://doi.org/10.4014/jmb.2403.03058Wang, F.
, Ouyang, Y., Zhou, P.
, Zhang, Y., Gao, R.
, Eser, B. E. & Guo, Z. (2024).
NIR-accelerated cascade reaction for degradation of organophosphorus compounds by Au/PTE/ZIF-8: Cooperative effect and mechanism.
Catalysis Science & Technology,
14(12), 3424-3435.
https://doi.org/10.1039/D4CY00311JZhou, P.
, Zhang, Y., Liu, W.
, Jones, N. C., Hoffmann, S. V., Eser, B. E., Zhang, M.
, Ouyang, Y., Wang, F., Deng, Y., Zhang, M.
& Guo, Z. (2024).
Effect of Deep Eutectic Mixtures in Hydroxylation of Fatty Acids: A Correlation between Water Activity and Thermostability of FA-HY1.
ACS Sustainable Chemistry & Engineering,
12(5), 1918-1929.
https://doi.org/10.1021/acssuschemeng.3c05867Santner, P., Chanquia, S. N., Petrovai, N., Vig Benfeldt, F.
, Kara, S. & Eser, B. E. (2023).
Biocatalytic Conversion of Fatty Acids into Drop-in Biofuels: Towards Sustainable Energy Sources.
EFB Bioeconomy Journal,
3, Article 100049.
https://doi.org/10.1016/j.bioeco.2023.100049
T. M. Henehan, G., Ryan, B. J.
, Eser, B. E., Li, N.
, Guo, Z. & Kinsella, G. K. (2023).
Editorial: Green chemistry biocatalysis.
Frontiers in Bioengineering and Biotechnology,
11, Article 1158275.
https://doi.org/10.3389/fbioe.2023.1158275Zong, L.
, Zhang, Y., Shao, Z., Ljubic, A., Jacobsen, C., Gao, R.
, Eser, B. E., Wang, Y., Wang, Y.
& Guo, Z. (2023).
Selective and Sustainable Production of Sub-terminal Hydroxy Fatty Acids by a Self-Sufficient CYP102 Enzyme from Bacillus Amyloliquefaciens.
ChemBioChem,
24(18), Article e202300368.
https://doi.org/10.1002/cbic.202300368Mi, H. T. N., Chaiyasarn, S.
, Eser, B. E., Tan, S. R. S., Burapan, S. & Han, J. (2022).
Allyl Aryl Ether Cleavage by Blautia sp. MRG-PMF1 Cocorrinoid O-Demethylase.
Microbiology Spectrum,
10(5).
https://doi.org/10.1128/spectrum.03305-22Nahuel Chanquia, S., Vig Benfeldt, F., Petrovai, N.
, Santner, P., Hollmann, F.
, Eser, B. E. & Kara, S. (2022).
Immobilization and Application of Fatty Acid Photodecarboxylase in Deep Eutectic Solvents.
ChemBioChem,
23(23), Article e202200482.
https://doi.org/10.1002/cbic.202200482 Zhang, X., Huang, Z., Wang, D.
, Zhang, Y., Eser, B. E., Gu, Z.
, Dai, R., Gao, R.
& Guo, Z. (2022).
A new thermophilic extradiol dioxygenase promises biodegradation of catecholic pollutants.
Journal of Hazardous Materials,
422, Article 126860.
https://doi.org/10.1016/j.jhazmat.2021.126860Zhang, Y., Breum, N. M. D., Schubert, S., Hashemi, N., Kyhnau, R., Knauf, M. S., Mathialakan, M., Takeuchi, M., Kishino, S., Ogawa, J., Kristensen, P.
, Guo, Z. & Eser, B. E. (2022).
Semi-rational Engineering of a Promiscuous Fatty Acid Hydratase for Alteration of Regioselectivity.
ChemBioChem,
23(4), Article e202100606.
https://doi.org/10.1002/cbic.202100606
Santner, P., Szabó, L. K.
, Chanquia, S. N., Høj Merrild, A., Hollmann, F.
, Kara, S. & Eser, B. E. (2021).
Optimization and Engineering of Fatty Acid Photodecarboxylase for Substrate Specificity.
ChemCatChem,
13(18), 4038-4046.
https://doi.org/10.1002/cctc.202100840
Zhang, Y., Eser, B. E., Kougioumtzoglou, G., Eser, Z., Poborsky, M., Kishino, S., Takeuchi, M., Ogawa, J., Kristensen, P.
& Guo, Z. (2021).
Effects of the engineering of a single binding pocket residue on specificity and regioselectivity of hydratases from Lactobacillus Acidophilus.
Biochemical Engineering Journal,
171, Article 108006.
https://doi.org/10.1016/j.bej.2021.108006
Zong, L., Gao, R.
, Guo, Z., Shao, Z., Wang, Y.
& Eser, B. E. (2021).
Characterization and modification of two self-sufficient CYP102 family enzymes from Bacillus amyloliquefaciens DSM 7 with distinct regioselectivity towards fatty acid hydroxylation.
Biochemical Engineering Journal,
166, Article 107871.
https://doi.org/10.1016/j.bej.2020.107871
Zong, L., Zhang, Y., Shao, Z., Wang, Y.
, Guo, Z., Gao, R.
& Eser, B. E. (2021).
Optimization and Engineering of a Self-Sufficient CYP102 Enzyme from Bacillus amyloliquefaciens towards Synthesis of In-Chain Hydroxy Fatty Acids.
Catalysts,
11(6), Article 665.
https://doi.org/10.3390/catal11060665
Burapan, S., Kim, M., Paisooksantivatana, Y.
, Eser, B. E. & Han, J. (2020).
Thai Curcuma species: Antioxidant and bioactive compounds.
Foods,
9(9), Article 1219.
https://doi.org/10.3390/foods9091219Eser, B. E., Poborsky, M., Dai, R., Kishino, S., Ljubic, A., Takeuchi, M., Jacobsen, C., Ogawa, J., Kristensen, P.
& Guo, Z. (2020).
Rational Engineering of Hydratase from Lactobacillus Acidophilus Reveals Critical Residues Directing Substrate Specificity and Regioselectivity.
ChemBioChem,
21(4), 550-563.
https://doi.org/10.1002/cbic.201900389
Li, J., Ma, Y., Liu, N.
, Eser, B. E., Guo, Z., Jensen, P. R. & Stephanopolos, G. (2020).
Synthesis of high-titer alka(e)nes in Yarrowia lipolytica is enabled by a discovered mechanism.
Nature Communications,
11(1), Article 6198 .
https://doi.org/10.1038/s41467-020-19995-0Eser, B. E., Zhang, X., Chanani, P. K., Begley, T. P. & Ealick, S. E. (2016).
From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis.
Journal of the American Chemical Society,
138(11), 3639-42.
https://doi.org/10.1021/jacs.6b00445
Zhang, X.
, Eser, B. E., Chanani, P. K., Begley, T. P. & Ealick, S. E. (2016).
Structural Basis for Iron-Mediated Sulfur Transfer in Archael and Yeast Thiazole Synthases.
Biochemistry,
55(12), 1826-38.
https://doi.org/10.1021/acs.biochem.6b00030McCracken, J.
, Eser, B. E., Mannikko, D., Krzyaniak, M. D. & Fitzpatrick, P. F. (2015).
HYSCORE Analysis of the Effects of Substrates on Coordination of Water to the Active Site Iron in Tyrosine Hydroxylase.
Biochemistry,
54(24), 3759-71.
https://doi.org/10.1021/acs.biochem.5b00363Krzyaniak, M. D.
, Eser, B. E., Ellis, H. R., Fitzpatrick, P. F. & McCracken, J. (2013).
Pulsed EPR study of amino acid and tetrahydropterin binding in a tyrosine hydroxylase nitric oxide complex: evidence for substrate rearrangements in the formation of the oxygen-reactive complex.
Biochemistry,
52(47), 8430-41.
https://doi.org/10.1021/bi4010914Eser, B. E., Das, D., Han, J., Jones, P. R. & Marsh, E. N. G. (2012).
Erratum: Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: Investigation of kinetics and requirement for an external electron donor (Biochemistry (2011) 50:49 (10743-10750). DOI: 10.1021/bi2012417).
Biochemistry,
51(28), 5703.
https://doi.org/10.1021/bi300837j
Das, D.
, Eser, B. E., Han, J., Sciore, A. & Marsh, E. N. G. (2011).
Oxygen-independent decarbonylation of aldehydes by cyanobacterial aldehyde decarbonylase: a new reaction of diiron enzymes.
Angewandte Chemie International Edition,
50(31), 7148-52.
https://doi.org/10.1002/anie.201101552Eser, B. E., Das, D., Han, J., Jones, P. R. & Marsh, E. N. G. (2011).
Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: investigation of kinetics and requirement for an external electron donor.
Biochemistry,
50(49), 10743-50.
https://doi.org/10.1021/bi2012417
Chow, M. S.
, Eser, B. E., Wilson, S. A., Hodgson, K. O., Hedman, B., Fitzpatrick, P. F. & Solomon, E. I. (2009).
Spectroscopy and kinetics of wild-type and mutant tyrosine hydroxylase: mechanistic insight into O2 activation.
Journal of the American Chemical Society,
131(22), 7685-98.
https://doi.org/10.1021/ja810080cEser, B. E., Barr, E. W., Frantom, P. A., Saleh, L., Bollinger, J. M., Krebs, C. & Fitzpatrick, P. F. (2007).
Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase.
Journal of the American Chemical Society,
129(37), 11334-5.
https://doi.org/10.1021/ja074446s
