Wei-Chen Chang

Bashiri, G., Bulloch, E. M. M., Bramley, W. R., Davidson, M., Stuteley, S. M., Young, P. G., … Squire, C. J. (2024). Poly-γ-glutamylation of biomolecules. NATURE COMMUNICATIONS, 15(1). https://doi.org/10.1038/s41467-024-45632-1

Chen, T.-Y., Chen, J., Ruszczycky, M. W., Hilovsky, D., Hostetler, T., Liu, X., … Chang, W.-chen. (2024, March 19). Variation in Biosynthesis and Metal-Binding Properties of Isonitrile-Containing Peptides Produced by Mycobacteria versus Streptomyces. ACS CATALYSIS, Vol. 3. https://doi.org/10.1021/acscatal.4c00645

Gering, H. E., Li, X., Tang, H., Swartz, P. D., Chang, W.-C., & Makris, T. M. (2023). A Ferric-Superoxide Intermediate Initiates P450-Catalyzed Cyclic Dipeptide Dimerization. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 8. https://doi.org/10.1021/jacs.3c04542

Paris, J. C., Hu, S., Wen, A., Weitz, A. C., Cheng, R., Gee, L. B., … Guo, Y. (2023, September 13). An <i>S</i>=1 Iron(IV) Intermediate Revealed in a Non-Heme Iron Enzyme-Catalyzed Oxidative C-S Bond Formation. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, Vol. 9. https://doi.org/10.1002/anie.202309362

Canty, N. K., & Chang, W.-chen. (2023). [Review of Current understanding of lignan biosynthesis]. ARKIVOC. https://doi.org/10.24820/ark.5550190.p012.006

Phan, H. N., Manley, O. M., Skirboll, S. S., Cha, L., Hilovsky, D., Chang, W.-chen, … Makris, T. M. (2023). Excision of a Protein-Derived Amine for <i>p</i>-Aminobenzoate Assembly by the Self-Sacrificial Heterobimetallic Protein CADD. BIOCHEMISTRY, 62(22), 3276–3282. https://doi.org/10.1021/acs.biochem.3c00406

Ushimaru, R., Cha, L., Shimo, S., Li, X., Paris, J. C., Mori, T., … Abe, I. (2023). Mechanistic Analysis of Stereodivergent Nitroalkane Cyclopropanation Catalyzed by Nonheme Iron Enzymes. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 145(44), 24210–24217. https://doi.org/10.1021/jacs.3c08413

Cha, L., Paris, J. C., Zanella, B., Spletzer, M., Yao, A., Guo, Y., & Chang, W.-chen. (2023, March 13). Mechanistic Studies of Aziridine Formation Catalyzed by Mononuclear Non-Heme Iron Enzymes. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol. 3. https://doi.org/10.1021/jacs.2c12664

Wang, B., Lu, Y., Cha, L., Chen, T.-Y., Palacios, P. M., Li, L., … Chen, C. (2023, September 6). Repurposing Iron- and 2-Oxoglutarate-Dependent Oxygenases to Catalyze Olefin Hydration. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, Vol. 9. https://doi.org/10.1002/anie.202311099

Chen, T.-Y., Zheng, Z., Zhang, X., Chen, J., Cha, L., Tang, Y., … Chang, W.-chen. (2022). Deciphering the Reaction Pathway of Mononuclear Iron Enzyme-Catalyzed N C Triple Bond Formation in Isocyanide Lipopeptide and Polyketide Biosynthesis. ACS CATALYSIS, 12(4), 2270–2279. https://doi.org/10.1021/acscatal.1c04869

Kim, W., Chen, T.-Y., Cha, L., Zhou, G., Xing, K., Canty, N. K., … Chang, W.-C. (2022). Elucidation of divergent desaturation pathways in the formation of vinyl isonitrile and isocyanoacrylate. NATURE COMMUNICATIONS, 13(1). https://doi.org/10.1038/s41467-022-32870-4

Li, X., Xue, S., Guo, Y., & Chang, W.-C. (2022). Mechanism of Methyldehydrofosmidomycin Maturation: Use Olefination to Enable Chain Elongation. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 144(18), 8257–8266. https://doi.org/10.1021/jacs.2c01924

Tang, H., Wu, M.-H., Lin, H.-Y., Han, M.-R., Tu, Y.-H., Yang, Z.-J., … Chang, W.-chen. (2022). Mechanistic analysis of carbon-carbon bond formation by deoxypodophyllotoxin synthase. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 119(1). https://doi.org/10.1073/pnas.2113770119

Manley, O. M., Phan, H. N., Stewart, A. K., Mosley, D. A., Xue, S., Cha, L., … Makris, T. M. (2022). Self-sacrificial tyrosine cleavage by an Fe:Mn oxygenase for the biosynthesis of para-aminobenzoate in Chlamydia trachomatis. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 119(39). https://doi.org/10.1073/pnas.2210908119

Chen, T.-Y., & Chang, W.-chen. (2021, July 13). A postreplicative C5-cytosine hypermodification triggered by bacteriophage methyltransferase and hydroxylase. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol. 118. https://doi.org/10.1073/pnas.2109992118

Manley, O. M., Tang, H., Xue, S., Guo, Y., Chang, W.-chen, & Makris, T. M. (2021, December 13). BesC Initiates C-C Cleavage through a Substrate-Triggered and Reactive Diferric-Peroxo Intermediate. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol. 12. https://doi.org/10.1021/jacs.1c11109

Chen, T.-Y., Chen, J., Tang, Y., Zhou, J., Guo, Y., & Chang, W.-chen. (2021). Current Understanding toward Isonitrile Group Biosynthesis and Mechanism. CHINESE JOURNAL OF CHEMISTRY, 39(2), 463–472. https://doi.org/10.1002/cjoc.202000448

Chen, T.-Y., Xue, S., Tsai, W.-C., Chien, T.-C., Guo, Y., & Chang, W.-chen. (2021). Deciphering Pyrrolidine and Olefin Formation Mechanism in Kainic Acid Biosynthesis. ACS CATALYSIS, 11(1), 278–282. https://doi.org/10.1021/acscatal.0c03879

Tang, H., Tang, Y., Kurnikov, I. V., Liao, H.-J., Chan, N.-L., Kurnikova, M. G., … Chang, W.-chen. (2021). Harnessing the Substrate Promiscuity of Dioxygenase AsqJ and Developing Efficient Chemoenzymatic Synthesis for Quinolones. ACS CATALYSIS, 11(12), 7186–7192. https://doi.org/10.1021/acscatal.1c01150

Li, X., Shimaya, R., Dairi, T., Chang, W.-chen, & Ogasawara, Y. (2021, December 27). Identification of Cyclopropane Formation in the Biosyntheses of Hormaomycins and Belactosins: Sequential Nitration and Cyclopropanation by Metalloenzymes. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, Vol. 12. https://doi.org/10.1002/anie.202113189

Cha, L., Milikisiyants, S., Davidson, M., Xue, S., Smirnova, T. I., Smirnov, A. I., … Chang, W.-C. (2020). Alternative Reactivity of Leucine 5-Hydroxylase Using an Olefin-Containing Substrate to Construct a Substituted Piperidine Ring. BIOCHEMISTRY, 59(21), 1961–1965. https://doi.org/10.1021/acs.biochem.0c00289

Cha, L., & Chang, W.-chen. (2020, December). An Effective Strategy to Introduce Carbon Isotopes by Simple Swaps of CO2. TRENDS IN CHEMISTRY, Vol. 2, pp. 1040–1042. https://doi.org/10.1016/j.trechm.2020.10.004

Li, J., Liao, H.-J., Tang, Y., Huang, J.-L., Cha, L., Lin, T.-S., … Guo, Y. (2020). Epoxidation Catalyzed by the Nonheme Iron(II)- and 2-Oxoglutarate-Dependent Oxygenase, AsqJ: Mechanistic Elucidation of Oxygen Atom Transfer by a Ferryl Intermediate. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 142(13), 6268–6284. https://doi.org/10.1021/jacs.0c00484

Chen, T.-Y., Chen, J., Tang, Y., Zhou, J., Guo, Y., & Chang, W.-chen. (2020). Pathway from N-Alkylglycine to Alkylisonitrile Catalyzed by Iron(II) and 2-Oxoglutarate-Dependent Oxygenases. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 59(19), 7367–7371. https://doi.org/10.1002/anie.201914896

Rajkovich, L. J., Pandelia, M.-E., Mitchell, A. J., Chang, W.-chen, Zhang, B., Boal, A. K., … Bollinger, J. M., Jr. (2019). A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases. BIOCHEMISTRY, 58(12), 1627–1647. https://doi.org/10.1021/acs.biochem.9b00044

Chang, W.-chen, Yang, Z.-J., Tu, Y.-H., & Chien, T.-C. (2019). Reaction Mechanism of a Nonheme Iron Enzyme Catalyzed Oxidative Cyclization via C-C Bond Formation. ORGANIC LETTERS, 21(1), 228–232. https://doi.org/10.1021/acs.orglett.8b03670

Davidson, M., McNamee, M., Fan, R., Guo, Y., & Chang, W.-chen. (2019). Repurposing Nonheme Iron Hydroxylases To Enable Catalytic Nitrile Installation through an Azido Group Assistance. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 141(8), 3419–3423. https://doi.org/10.1021/jacs.8b13906

Thibodeaux, C. J., Chang, W.-chen, & Liu, H.-wen. (2019). Unraveling flavoenzyme reaction mechanisms using flavin analogues and linear free energy relationships. NEW APPROACHES FOR FLAVIN CATALYSIS, Vol. 620, pp. 167–188. https://doi.org/10.1016/bs.mie.2019.03.010

Yu, C.-P., Tang, Y., Cha, L., Milikisiyants, S., Smirnova, T. I., Smirnov, A. I., … Chang, W.-chen. (2018). Elucidating the Reaction Pathway of Decarboxylation-Assisted Olefination Catalyzed by a Mononuclear Non-Heme Iron Enzyme. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 140(45), 15190–15193. https://doi.org/10.1021/jacs.8b10077

Liao, H.-J., Li, J., Huang, J.-L., Davidson, M., Kurnikov, I., Lin, T.-S., … Chang, W.-chen. (2018). Insights into the Desaturation of Cyclopeptin and its C3 Epimer Catalyzed by a non-Heme Iron Enzyme: Structural Characterization and Mechanism Elucidation. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 57(7), 1831–1835. https://doi.org/10.1002/anie.201710567

Pan, J., Bhardwaj, M., Zhang, B., Chang, W.-chen, Schardl, C. L., Krebs, C., … Bollinger, J. M., Jr. (2018). Installation of the Ether Bridge of Lolines by the Iron- and 2-Oxoglutarate-Dependent Oxygenase, LolO: Regio- and Stereochemistry of Sequential Hydroxylation and Oxacyclization Reactions. Biochemistry, 57(14), 2074–2083. https://doi.org/10.1021/ACS.BIOCHEM.8B00157

Chang, W.-chen, Liu, P., & Guo, Y. (2018). Mechanistic Elucidation of Two Catalytically Versatile Iron(II)- and -Ketoglutarate-Dependent Enzymes: Cases Beyond Hydroxylation. COMMENTS ON INORGANIC CHEMISTRY, 38(4), 127–165. https://doi.org/10.1080/02603594.2018.1509856

Huang, J.-L., Tang, Y., Yu, C.-P., Sanyal, D., Jia, X., Liu, X., … Chang, W.-chen. (2018). Mechanistic Investigation of Oxidative Decarboxylation Catalyzed by Two Iron(II)- and 2-Oxoglutarate-Dependent Enzymes. BIOCHEMISTRY, 57(12), 1838–1841. https://doi.org/10.1021/acs.biochem.8b00115

Rose, H. R., Ghosh, M. K., Maggiolo, A. O., Pollock, C. J., Blaesi, E. J., Hajj, V., … Boal, A. K. (2018). Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class i Ribonucleotide Reductase and for Radical Initiation by Its Dimanganese Cofactor. Biochemistry, 57(18), 2679–2693. https://doi.org/10.1021/acs.biochem.8b00247

Ushimaru, R., Ruszczycky, M. W., Chang, W.-chen, Yan, F., Liu, Y.-nan, & Liu, H.-wen. (2018). Substrate Conformation Correlates with the Outcome of Hyoscyamine 6β-Hydroxylase Catalyzed Oxidation Reactions. Journal of the American Chemical Society, 140(24), 7433–7436. https://doi.org/10.1021/JACS.8B03729

Dunham, N. P., Chang, W.-chen, Mitchell, A. J., Martinie, R. J., Zhang, B., Bergman, J. A., … Bollinger, J. M., Jr. (2018). Two Distinct Mechanisms for C-C Desaturation by Iron(II)- and 2-(Oxo)glutarate-Dependent Oxygenases: Importance of alpha-Heteroatom Assistance. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 140(23), 7116–7126. https://doi.org/10.1021/jacs.8b01933

Chang, W.-C., Sanyal, D., Huang, J.-L., Ittiamornkui, K., Zhu, Q., & Liu, X. (2017). In Vitro Stepwise Reconstitution of Amino Acid Derived Vinyl Isocyanide Biosynthesis: Detection of an Elusive Intermediate. ORGANIC LETTERS, 19(5), 1208–1211. https://doi.org/10.1021/acs.orglett.7b00258

Mitchell, A. J., Dunham, N. P., Bergman, J. A., Wang, B., Zhu, Q., Chang, W.-chen, … Boal, A. K. (2017). Structure-Guided Reprogramming of a Hydroxylase To Halogenate Its Small Molecule Substrate. BIOCHEMISTRY, 56(3), 441–444. https://doi.org/10.1021/acs.biochem.6b01173

Mitchell, A. J., Dipham, N. P., Martinie, R. J., Bergman, J. A., Pollock, C. J., Hu, K., … Boal, A. K. (2017). Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 139(39), 13830–13836. https://doi.org/10.1021/jacs.7b07374

Chang, W.-chen, Li, J., Lee, J. L., Cronican, A. A., & Guo, Y. (2016). Mechanistic Investigation of a Non-Heme Iron Enzyme Catalyzed Epoxidation in (-)-4 '-Methoxycyclopenin Biosynthesis. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 138(33), 10390–10393. https://doi.org/10.1021/jacs.6b05400

Tamanaha, E., Zhang, B., Guo, Y., Chang, W.-chen, Barr, E. W., Xing, G., … Krebs, C. (2016). Spectroscopic Evidence for the Two C–H-Cleaving Intermediates of Aspergillus nidulans Isopenicillin N Synthase. Journal of the American Chemical Society, 138(28), 8862–8874. https://doi.org/10.1021/jacs.6b04065

Boal, A. K., Bollinger, J. M., Jr., & Chang, W.-chen. (2015). Assembly of the unusual oxacycles in the orthosomycin antibiotics. Proceedings of the National Academy of Sciences, 112(39), 11989–11990. https://doi.org/10.1073/pnas.1514689112

Martinie, R. J., Livada, J., Chang, W.-C., Green, M. T., Krebs, C., Bollinger, J. M., & Silakov, A. (2015). Experimental correlation of substrate position with reaction outcome in the aliphatic halogenase, SyrB2. Journal of the American Chemical Society, 137(21), 6912–6919. https://doi.org/10.1021/jacs.5b03370

Bollinger, J. M., Chang, W.-C., Matthews, M. L., Martinie, R. J., Boal, A. K., & Krebs, C. (2015). Mechanisms of 2-oxoglutarate-dependent oxygenases: The hydroxylation paradigm and beyond. In RSC Metallobiology: Vol. 2015-January (pp. 95–122). https://doi.org/10.1039/9781782621959-00095

Rajakovich, L. J., Nørgaard, H., Warui, D. M., Chang, W.-chen, Li, N., Booker, S. J., … Pandelia, M.-E. (2015). Rapid Reduction of the Diferric-Peroxyhemiacetal Intermediate in Aldehyde-Deformylating Oxygenase by a Cyanobacterial Ferredoxin: Evidence for a Free-Radical Mechanism. Journal of the American Chemical Society, 137(36), 11695–11709. https://doi.org/10.1021/jacs.5b06345

Matthews, M. L., Chang, W.-chen, Layne, A. P., Miles, L. A., Krebs, C., & Bollinger, J. M., Jr. (2014). Direct nitration and azidation of aliphatic carbons by an iron-dependent halogenase. Nature Chemical Biology, 10(3), 209–215. https://doi.org/10.1038/nchembio.1438

Mechanism of the C5 stereoinversion reaction in the biosynthesis of carbapenem antibiotics. (2014). Science, 343(6175), 1140–1144. https://doi.org/10.1126/science.1248000

Huang, H., Chang, W.-C., Lin, G.-M., Romo, A., Pai, P.-J., Russell, W. K., … Liu, H.-W. (2014). Mechanistic Consequences of Chiral Radical Clock Probes: Analysis of the Mononuclear Non-Heme Iron Enzyme HppE with 2-Hydroxy-3-methylenecyclopropyl Radical Clock Substrates. Journal of the American Chemical Society, 136(8), 2944–2947. https://doi.org/10.1021/ja4100035

Chang, W.-chen, Song, H., Liu, H.-wen, & Liu, P. (2013). Current development in isoprenoid precursor biosynthesis and regulation. Current Opinion in Chemical Biology, 17(4), 571–579. https://doi.org/10.1016/j.cbpa.2013.06.020

Evidence that the fosfomycin-producing epoxidase, HppE, is a non-heme-iron peroxidase. (2013). Science, 342(6161), 991–995. https://doi.org/10.1126/science.1240373

Chang, W.-chen, Dey, M., Liu, P., Mansoorabadi, S. O., Moon, S.-J., Zhao, Z. K., … Liu, H.-wen. (2013). Mechanistic studies of an unprecedented enzyme-catalysed 1,2-phosphono-migration reaction. Nature, 496(7443), 114–118. https://doi.org/10.1038/nature11998

Zhao, L., Chang, W.-C., Xiao, Y., Liu, H.-W., & Liu, P. (2013). Methylerythritol phosphate pathway of isoprenoid biosynthesis. In Annual Review of Biochemistry (Vol. 82, pp. 497–530). https://doi.org/10.1146/annurev-biochem-052010-100934

Chang, W.-chen, Mansoorabadi, S. O., & Liu, H.-wen. (2013). Reaction of HppE with Substrate Analogues: Evidence for Carbon–Phosphorus Bond Cleavage by a Carbocation Rearrangement. Journal of the American Chemical Society, 135(22), 8153–8156. https://doi.org/10.1021/ja403441x

Pandelia, M. E., Li, N., Nørgaard, H., Warui, D. M., Rajakovich, L. J., Chang, W.-chen, … Bollinger, J. M., Jr. (2013). Substrate-Triggered Addition of Dioxygen to the Diferrous Cofactor of Aldehyde-Deformylating Oxygenase to Form a Diferric-Peroxide Intermediate. Journal of the American Chemical Society, 135(42), 15801–15812. https://doi.org/10.1021/ja405047b

Thibodeaux, C. J., Chang, W.-chen, & Liu, H.-wen. (2012). Enzymatic Chemistry of Cyclopropane, Epoxide, and Aziridine Biosynthesis. Chemical Reviews, 112(3), 1681–1709. https://doi.org/10.1021/cr200073d

Li, N., Chang, W.-chen, Warui, D. M., Booker, S. J., Krebs, C., & Bollinger, J. M., Jr. (2012). Evidence for Only Oxygenative Cleavage of Aldehydes to Alk(a/e)nes and Formate by Cyanobacterial Aldehyde Decarbonylases. Biochemistry, 51(40), 7908–7916. https://doi.org/10.1021/bi300912n

Huang, H., Chang, W.-chen, Pai, P.-J., Romo, A., Mansoorabadi, S. O., Russell, D. H., & Liu, H.-wen. (2012). Evidence for Radical-Mediated Catalysis by HppE: A Study Using Cyclopropyl and Methylenecyclopropyl Substrate Analogues. Journal of the American Chemical Society, 134(39), 16171–16174. https://doi.org/10.1021/ja3078126

Sun, H. G., Ruszczycky, M. W., Chang, W.-chen, Thibodeaux, C. J., & Liu, H.-wen. (2012). Nucleophilic Participation of Reduced Flavin Coenzyme in Mechanism of UDP-galactopyranose Mutase. Journal of Biological Chemistry, 287(7), 4602–4608. https://doi.org/10.1074/jbc.M111.312538

Chang, W.-chen, Xiao, Y., Liu, H.-wen, & Liu, P. (2011). Mechanistic Studies of an IspH-Catalyzed Reaction: Implications for Substrate Binding and Protonation in the Biosynthesis of Isoprenoids. Angewandte Chemie International Edition, 50(51), 12304–12307. https://doi.org/10.1002/anie.201104124

Xiao, Y., Chang, W.-chen, Liu, H.-wen, & Liu, P. (2011). Study of IspH, a Key Enzyme in the Methylerythritol Phosphate Pathway Using Fluoro-Substituted Substrate Analogues. Organic Letters, 13(21), 5912–5915. https://doi.org/10.1021/ol202559r

Thibodeaux, C. J., Chang, W.-chen, & Liu, H.-wen. (2010). Linear Free Energy Relationships Demonstrate a Catalytic Role for the Flavin Mononucleotide Coenzyme of the Type II Isopentenyl Diphosphate:Dimethylallyl Diphosphate Isomerase. Journal of the American Chemical Society, 132(29), 9994–9996. https://doi.org/10.1021/ja104090m

Thibodeaux, C. J., Mansoorabadi, S. O., Kittleman, W., Chang, W.-chen, & Liu, H.-wen. (2008). Evidence for the Involvement of Acid/Base Chemistry in the Reaction Catalyzed by the Type II Isopentenyl Diphosphate/Dimethylallyl Diphosphate Isomerase fromStaphylococcus aureus. Biochemistry, 47(8), 2547–2558. https://doi.org/10.1021/bi701467g

Munos, J. W., Moon, S.-J., Mansoorabadi, S. O., Chang, W., Hong, L., Yan, F., … Liu, H.-wen. (2008). Purification and Characterization of the Epoxidase Catalyzing the Formation of Fosfomycin from Pseudomonas syringae. Biochemistry, 47(33), 8726–8735. https://doi.org/10.1021/bi800877v