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, Santner, P., Szabó, L. K.
, Madsen, J. S., Øhlenschlæger, M. L., Sarvari, A. G.
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, 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
Mi, 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.2403.03058
Wang, 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/D4CY00311J
Zhou, 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.3c05867
Santner, 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, Artikel 100049. Advance online publication.
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, Artikel 1158275.
https://doi.org/10.3389/fbioe.2023.1158275
Zong, 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), Artikel e202300368.
https://doi.org/10.1002/cbic.202300368
Nahuel 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), Artikel e202200482.
https://doi.org/10.1002/cbic.202200482
Zhang, 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), Artikel e202100606.
https://doi.org/10.1002/cbic.202100606
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, Artikel 126860.
https://doi.org/10.1016/j.jhazmat.2021.126860
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, Artikel 108006.
https://doi.org/10.1016/j.bej.2021.108006
Zong, L., Gao, R.
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& 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, Artikel 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), Artikel 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), Artikel 1219.
https://doi.org/10.3390/foods9091219
Eser, 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), Artikel 6198 .
https://doi.org/10.1038/s41467-020-19995-0
Eser, 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.6b00030
McCracken, 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.5b00363
Krzyaniak, 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/bi4010914
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.201101552
Eser, 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.
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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/ja810080c
Eser, 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