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Stereoselective amino acid synthesis by synergistic photoredox-pyridoxal radical biocatalysis
Open accessAbstract
Developing synthetically useful enzymatic reactions that are not known in biochemistry and organic chemistry is an important challenge in biocatalysis. Through the synergistic merger of photoredox catalysis and pyridoxal 5′-phosphate (PLP) biocatalysis, we developed a pyridoxal radical biocatalysis approach to prepare valuable noncanonical amino acids, including those bearing a stereochemical dyad or triad, without the need for protecting groups. Using engineered PLP enzymes, either enantiomeric product could be produced in a biocatalyst-controlled fashion. Synergistic photoredox - pyridoxal radical biocatalysis represents a powerful platform with which to discover previously unknown catalytic reactions and to tame radical intermediates for asymmetric catalysis.
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Cites
Density-functional thermochemistry. III. The role of exact exchange
Becke, A. D. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464913 · Cited by 103,767
Lee, C., Yang, W., & Parr, R. G. (1988) · Physical Review B · doi:10.1103/physrevb.37.785 · Cited by 100,874
Grimme, S., Antony, J., Ehrlich, S., & Krieg, H. (2010) · The Journal of Chemical Physics · doi:10.1063/1.3382344 · Cited by 59,686
Density-functional exchange-energy approximation with correct asymptotic behavior
Becke, A. D. (1988) · Physical Review A · doi:10.1103/physreva.38.3098 · Cited by 54,100
Comparison of simple potential functions for simulating liquid water
Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,397
Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems
Darden, T., York, D., & Pedersen, L. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464397 · Cited by 29,638
AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
Morris, G. M., Huey, R., Lindstrom, W., Sanner, M. F., Belew, R. K., Goodsell, D. S., & Olson, A. J. (2009) · Journal of Computational Chemistry · doi:10.1002/jcc.21256 · Cited by 26,294
Ryckaert, J.-P., Ciccotti, G., & Berendsen, H. J. C. (1977) · Journal of Computational Physics · doi:10.1016/0021-9991(77)90098-5 · Cited by 21,430
Development and testing of a general amber force field
Wang, J.-M., Wolf, R., Caldwell, J., Kollman, P., & Case, D. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20035 · Cited by 18,318
Marenich, A. V., Cramer, C. J., & Truhlar, D. G. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp810292n · Cited by 18,213
Cited by
Sorted by citations
Items 201–253 of 253
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Wang, H., & Ye, Y. (2023) · Chem Catalysis · doi:10.1016/j.checat.2023.100753
Bande, A., Barra, L., Blasco, E., Heine, J., Jahn, U., Meermann, B., Strub, E., & Tambornino, F. (2023) · Nachrichten aus der Chemie · doi:10.1002/nadc.20234136126
List, B., & Poje, M. M. (2023) · Synfacts · doi:10.1055/s-0042-1752035
Zanda, M. (2023) · Synthesis · doi:10.1055/s-0040-1720617
Zanda, M. (2023) · Synlett · doi:10.1055/s-0040-1720616
Zanda, M. (2023) · Synfacts · doi:10.1055/s-0040-1720615
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Liu, S., Yeh, C., Reavill, C., Jones, B., Zou, Y., & Hai, Y. (2024) · Angewandte Chemie · doi:10.1002/ange.202317161
Bork, H., Naße, K. E., Vorholt, A. J., & Gröger, H. (2024) · Angewandte Chemie · doi:10.1002/ange.202401989
Garcha, J., Huang, J., Pomier, K. M., & Melacini, G. (2024) · Biophysical Chemistry · doi:10.1016/j.bpc.2024.107320
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Ting, C. P., & Singh, B. (2024) · Synlett · doi:10.1055/a-2500-7798
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Guo, J., Wu, Y., & Zhong, F. (2025) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2025.08.005
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Rui, J., Mu, X., & Huang, X. (2025) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2025.08.017
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Studinski, C. I., Powers, M., Martin, B. K., Mosconi, A. L., Abraham, J. J., Koss, K. R., Bruffy, S. K., Campbell, M. E., Buller, A. R., & Willoughby, P. H. (2025) · ACS Omega · doi:10.1021/acsomega.5c07519
Deciphering genetic susceptibility to clear cell renal cell carcinoma
Mandelia, M., Law, P., Mills, C., Went, M., Vijayakrishnan, J., & Houlston, R. S. (2025) · Communications Biology · doi:10.1038/s42003-025-09297-w
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Fan, Y., Chen, J., Fan, Z., Chirinos, J. A., Stein, J. L., Sullivan, P. F., Wang, R., Nadig, A., Zhang, D. Y., Huang, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-67431-y · Cited by 1
Abolhassani, A., Alawathurage, T. M., Schmidt, A., Brand, F., Kilarski, L. L., Altmann, H., Dahl, E., Frank, S., Göpel, S., Hanses, F., et al. (2026) · Human Genomics · doi:10.1186/s40246-025-00904-9
Kato, S., Takeuchi, K., Umeda, K., Kudo, H., Hasunuma, T., & Hayashi, T. (2026) · Angewandte Chemie · doi:10.1002/ange.202526025
Brown, E. A., Varney, S., Young, A. E., Wolf, Z. T., Foreman, O., Wade, C. M., Hughes, A. M., Oberbauer, A. M., Safra, N., Lindblad‐Toh, K., et al. (2026) · Scientific Reports · doi:10.1038/s41598-026-42994-y
Dai, Z., Haque, B., Xi, S., & Costain, G. (2026) · Genome Medicine · doi:10.1186/s13073-026-01631-z
Kqiku, L., & Paradisi, F. (2026) · Current Opinion in Green and Sustainable Chemistry · doi:10.1016/j.cogsc.2026.101072
Akçimen, F., Díez-Fairén, M., Alvarez, I., Puente, V., Grant, S. M., Hernández‐Vara, J., Khani, M., Buongiorno, M., Jiménez-Jiménez, F. J., Agúndez, J. A. G., et al. (2026) · npj Genomic Medicine · doi:10.1038/s41525-026-00567-y · Cited by 1
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Kazdal, D. N., Budczies, J., Menzel, M., Altbürger, C., Kahles, A., Ourailidis, I., Brinkmöller, M., Schirmacher, P., & Stenzinger, A. (2026) · Die Pathologie · doi:10.1007/s00292-026-01571-w
Deng, Z., Jan, J. E. L., Padalino, M. A., Dekeyser, R., Dudding, T. C., & Johnston, J. N. (2026) · ACS Catalysis · doi:10.1021/acscatal.6c02140
Ran, Y., Cai, Q., Jiang, Y., Tou, Y., Wang, Y., & Yang, T. (2026) · Catalysts · doi:10.3390/catal16070640
Wang, C., Yu, J., Chen, H., Hu, W., Wang, H., Liang, Y. F., & Pan, H. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c05795
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Wang, X., Gao, Y., Chen, Y., Chen, H., Gao, X., Houk, K. N., & Liang, Y. F. (2026) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.70081 · Cited by 2
Wang, H., Mai, B. K., Zhang, X., Li, C., Liu, P., & Yang, Y. (2026) · Angewandte Chemie · doi:10.1002/ange.7251439
Self-citationWang, C., Yu, J., Ye, Y., & Pan, H. (2026) · Organic Chemistry Frontiers · doi:10.1039/d6qo00912c
ATP-free single-strain one-pot whole-cell bioconversion of pyridoxal 5′-phosphate from pyridoxine
周佳佳, Wei, W., Li, X., Hu, G., Gao, C., Liu, J., Zhang, Y., Zhou, Y., Wu, J., Liu, L., et al. (2026) · Green Chemistry · doi:10.1039/d6gc03538h
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Bai, Z., Zhou, Y., & Zhao, H. (2026) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2026.102756
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Feng, J., Zhu, C.-L., & Li, M. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5257-2_4
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Alenad, A., Zhang, Y., Al-Qattan, A. M., Aljohani, K., Ali, I., Li, G., & Zhao, Z. (2026) · Materials Today Catalysis · doi:10.1016/j.mtcata.2026.100158
Zheng, C., Mai, B. K., Way, R. Y., Liu, P., Zhu, Q., & Yang, Y. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c08663
Self-citationKuo, L.-H., Yang, J., & Arnold, F. H. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c14064
Liangshi, W., Yang, C., Ma, J., Hangbo, Z., Shen, Y., Yang, J., Yan, H., Zhang, Y., Ge, G., & Che, R. (2026) · Journal of Energy Chemistry · doi:10.1016/j.jechem.2026.09.028
Sheng, Y., & Zhou, Z. (2026) · Organic Letters · doi:10.1021/acs.orglett.6c03443
Recent Advances in Nitrogenative Cleavage and Remodeling of Carbon-Carbon Double Bonds in Alkenes
Xu, R., Shi, H., & Jiao, N. (2026) · Chinese Journal of Organic Chemistry · doi:10.6023/cjoc202604050
Liu, Y., Wang, S., Hu, W., Guo, H., Mahmood, Z., Liao, Y., Pan, Y., Wang, X., Wang, W., Zhang, Z., et al. (2026) · Science Advances · doi:10.1126/sciadv.aeg3842
Electron Donor–Acceptor Complex Catalysis in Synthetic Chemistry
von Münchow, T., Palone, A., Trimble, J. S., & Melchiorre, P. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.1736780
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Kim, R., Gruhin, J. N., Wu, X., Semenick, R. S., Vasilopoulos, A., Voight, E. A., Renata, H., & Alexanian, E. J. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c14950
Bo, Z., Cheng, L., Zhang, X., Singh, À., Liu, P., & Yang, Y. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.07.757362
Self-citationElectron Donor–Acceptor Complex Catalysis in Synthetic Chemistry
von Münchow, T., Palone, A., Trimble, J. S., & Melchiorre, P. (2026) · Angewandte Chemie · doi:10.1002/ange.1736780
Deng, Y., Shi, Y., Pang, T., Wu, G., Wu, Y., & Zhong, F. (2026) · ACS Catalysis · doi:10.1021/acscatal.6c06572
Zhao, L.-P., Mai, B. K., Guo, R., Cheng, L., Liu, H., Liu, H., Zhao, Y., Liu, P., & Yang, Y. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.15.759323
Self-citationRao, G., Zhang, Z., Liu, X., Shiau, A. A., Britt, R. D., & Yang, Y. (2026) · Journal of the American Chemical Society · doi:10.64898/2026.10.15.759499
Self-citationBo, Z., Cheng, L., Zhang, X., Singh, À., Liu, P., & Yang, Y. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c14337
Self-citationZhao, L.-P., Mai, B. K., Guo, R., Cheng, L., Liu, H., Lin, K., Zhao, Y., Liu, P., & Yang, Y. (2026) · Nature Catalysis · doi:10.1038/s41929-026-01629-1
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Chai, W., Lahiri, A., & Hai, Y. (2026) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2026.102809
Mou, K., Tian, Z., Xu, W., Kang, X., Ma, Y., Zhuang, P., Lu, Z., Zhang, J., Guo, Y., Xu, L., et al. (2026) · Nature Catalysis · doi:10.1038/s41929-026-01624-6
Metadata
- Authors
- Cheng, L., Li, D., Mai, B. K., Bo, Z., Cheng, L., Liu, P., & Yang, Y.
- Affiliations
- University of California, Santa Barbara (US)
- University of Pittsburgh (US)
- Corresponding author
- Liu, Peng
- Yang, Yang
- Venue
- Science
- Published
- 2023-07-28
- Volume
- 381
- Issue
- 6656
- Pages
- 444-451
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC10444520
- OpenAlex
- W4385298585
- Cited by
- 253
- References
- 123
- Citations by year
- 2026: 80 · 2025: 105 · 2024: 57 · 2023: 11
- FWCI
- 22.35
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation (1933487)
- University of Pittsburgh
- Herman Frasch Foundation for Chemical Research (947-HF22)
- Xiamen University
- National Institutes of Health
- University of California, Santa Barbara
- National Institute of General Medical Sciences (R35GM147387, R35GM128779)
- Division of Materials Research (. DMR-1933487, 1933487)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Physical Sciences › Chemistry › Organic Chemistry › Radical Photochemical Reactions
- Physical Sciences › Chemistry › Organic Chemistry › Asymmetric Synthesis and Catalysis
- Keywords
- unnatural amino acids, photoredox catalysis, asymmetric catalysis, radical intermediates, engineered enzymes
- MeSH terms
- Amino Acids, Pyridoxal Phosphate, Stereoisomerism, Biocatalysis
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