Stereoselective amino acid synthesis by synergistic photoredox-pyridoxal radical biocatalysis

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

Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density

Lee, C., Yang, W., & Parr, R. G. (1988) · Physical Review B · doi:10.1103/physrevb.37.785 · Cited by 100,874

A consistent and accurate ab initio parametrization of density functional dispersion correction (DFT-D) for the 94 elements H-Pu

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

Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes

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

Universal Solvation Model Based on Solute Electron Density and on a Continuum Model of the Solvent Defined by the Bulk Dielectric Constant and Atomic Surface Tensions

Marenich, A. V., Cramer, C. J., & Truhlar, D. G. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp810292n · Cited by 18,213

Long-range corrected hybrid density functionals with damped atom–atom dispersion corrections

Chai, J.-D., & Head-Gordon, M. (2008) · Physical Chemistry Chemical Physics · doi:10.1039/b810189b · Cited by 14,648

Enzymatic assembly of DNA molecules up to several hundred kilobases

Gibson, D. G., Young, L., Chuang, R.-Y., Venter, J. C., Hutchison, C. A., & Smith, H. O. (2009) · Nature Methods · doi:10.1038/nmeth.1318 · Cited by 10,088

Visible Light Photoredox Catalysis with Transition Metal Complexes: Applications in Organic Synthesis

Prier, C. K., Rankic, D. A., & MacMillan, D. W. C. (2013) · Chemical Reviews · doi:10.1021/cr300503r · Cited by 9,590

A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model

Bayly, C. I., Cieplak, P., Cornell, W. D., & Kollman, P. A. (1993) · The Journal of Physical Chemistry · doi:10.1021/j100142a004 · Cited by 8,152

Organic Photoredox Catalysis

Romero, N. A., & Nicewicz, D. A. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00057 · Cited by 6,407

Visible light photoredox catalysis: applications in organic synthesis

Narayanam, J. M. R., & Stephenson, C. R. J. (2010) · Chemical Society Reviews · doi:10.1039/b913880n · Cited by 4,198

An approach to computing electrostatic charges for molecules

Singh, U. C., & Kollman, P. A. (1984) · Journal of Computational Chemistry · doi:10.1002/jcc.540050204 · Cited by 3,461

Atomic charges derived from semiempirical methods

Besler, B. H., Merz, K. M., & Kollman, P. A. (1990) · Journal of Computational Chemistry · doi:10.1002/jcc.540110404 · Cited by 3,366

XSEDE: Accelerating Scientific Discovery

Towns, J. W., Cockerill, T. M., Dahan, M., Foster, I. T., Gaither, K., Grimshaw, A. S., Hazlewood, V., Lathrop, S. A., Lifka, D. A., Peterson, G. D., et al. (2014) · Computing in Science & Engineering · doi:10.1109/mcse.2014.80 · Cited by 3,114

Advances in molecular quantum chemistry contained in the Q-Chem 4 program package

Shao, Y., Gan, Z., Epifanovsky, E., Gilbert, A. T. B., Wormit, M., Kußmann, J., Lange, A. W., Behn, A., Deng, J., Feng, X., et al. (2014) · Molecular Physics · doi:10.1080/00268976.2014.952696 · Cited by 3,007

Dual Catalysis Strategies in Photochemical Synthesis

Skubi, K. L., Blum, T. R., & Yoon, T. P. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00018 · Cited by 2,722

Proton-Coupled Electron Transfer

Weinberg, D. R., Gagliardi, C. J., Hull, J. F., Murphy, C. F., Kent, C. A., Westlake, B. C., Paul, A., Ess, D. H., McCafferty, D. G., & Meyer, T. J. (2012) · Chemical Reviews · doi:10.1021/cr200177j · Cited by 2,462

CB-Dock2: improved protein–ligand blind docking by integrating cavity detection, docking and homologous template fitting

Liu, Y., Yang, X., Gan, J., Chen, S., Xiao, Z. J., & Cao, Y. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac394 · Cited by 2,255

Nature of biological electron transfer

Moser, C. C., Keske, J. M., Warncke, K., Farid, R., & Dutton, P. L. (1992) · Nature · doi:10.1038/355796a0 · Cited by 1,875

H++ 3.0: automating pK prediction and the preparation of biomolecular structures for atomistic molecular modeling and simulations

Anandakrishnan, R., Aguilar, B. H., & Onufriev, A. (2012) · Nucleic Acids Res. · doi:10.1093/nar/gks375 · Cited by 1,736

Determination ofD-amino acids. II. Use of a bifunctional reagent, 1,5-difluoro-2,4-dinitrobenzene

Marfey, P. S. (1984) · Carlsberg Research Communications · doi:10.1007/bf02908688 · Cited by 1,379

Single-electron transmetalation in organoboron cross-coupling by photoredox/nickel dual catalysis

Tellis, J. C., Primer, D. N., & Molander, G. A. (2014) · Science · doi:10.1126/science.1253647 · Cited by 1,295

Synergistic catalysis: A powerful synthetic strategy for new reaction development

Allen, A., & MacMillan, D. W. C. (2012) · Chemical Science · doi:10.1039/c2sc00907b · Cited by 1,211

ELECTRON TRANSFER IN PROTEINS

Gray, H. B., & Winkler, J. R. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.002541 · Cited by 1,046

Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations

Eliot, A. C., & Kirsch, J. F. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074021 · Cited by 955

Engineering new catalytic activities in enzymes

Chen, K., & Arnold, F. H. (2020) · Nature Catalysis · doi:10.1038/s41929-019-0385-5 · Cited by 879

Long-range electron transfer

Gray, H. B., & Winkler, J. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408029102 · Cited by 855

Catalytic Asymmetric Synthesis of α-Amino Acids

Nájera, C., & Sansano, J. M. (2007) · Chemical Reviews · doi:10.1021/cr050580o · Cited by 825

An algal photoenzyme converts fatty acids to hydrocarbons

Sorigué, D. R., Légeret, B., Cuiné, S., Blangy, S., Moulin, S., Billon, E., Richaud, P., Brugière, S., Couté, Y., Nurizzo, D., et al. (2017) · Science · doi:10.1126/science.aan6349 · Cited by 505

Absolute Potential of the Standard Hydrogen Electrode and the Problem of Interconversion of Potentials in Different Solvents

Isse, A. A., & Gennaro, A. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp100402x · Cited by 505

Designing logical codon reassignment – Expanding the chemistry in biology

Dumas, A., Lercher, L., Spicer, C. D., & Davis, B. G. (2014) · Chemical Science · doi:10.1039/c4sc01534g · Cited by 499

Thermodynamics of the Electron and the Proton

Bartmess, J. E. (1994) · The Journal of Physical Chemistry · doi:10.1021/j100076a029 · Cited by 492

Free Energies of Proton-Coupled Electron Transfer Reagents and Their Applications

Agarwal, R. G., Coste, S. C., Groff, B. D., Heuer, A. M., Noh, H., Parada, G. A., Wise, C. F., Nichols, E. M., Warren, J. J., & Mayer, J. M. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00521 · Cited by 490

Marfey?s reagent for chiral amino acid analysis: A review

Bhushan, R., & Br�ckner, H. (2004) · Amino Acids · doi:10.1007/s00726-004-0118-0 · Cited by 488

Recent Advances in the Theory and Molecular Simulation of Biological Electron Transfer Reactions

Blumberger, J. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00298 · Cited by 455

Accessing non-natural reactivity by irradiating nicotinamide-dependent enzymes with light

Emmanuel, M. A., Greenberg, N. R., Oblinsky, D. G., & Hyster, T. K. (2016) · Nature · doi:10.1038/nature20569 · Cited by 449

Photoexcitation of flavoenzymes enables a stereoselective radical cyclization

Biegasiewicz, K. F., Cooper, S. J., Gao, X., Oblinsky, D. G., Kim, J. H., Garfinkle, S. E., Joyce, L. A., Sandoval, B. A., Scholes, G. D., & Hyster, T. K. (2019) · Science · doi:10.1126/science.aaw1143 · Cited by 446

Alkylboronic Esters from Copper‐Catalyzed Borylation of Primary and Secondary Alkyl Halides and Pseudohalides

Yang, C., Zhang, Z., Tajuddin, H., Wu, C., Liang, J., Liu, J., Fu, Y., Czyzewska, M., Steel, P. G., Marder, T. B., et al. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201106299 · Cited by 422

Quantum Chemical Studies of Intermediates and Reaction Pathways in Selected Enzymes and Catalytic Synthetic Systems

Noodleman, L., Lovell, T., Han, W., Li, J., & Himo, F. (2004) · Chemical Reviews · doi:10.1021/cr020625a · Cited by 373

Photoenzymatic enantioselective intermolecular radical hydroalkylation

Huang, X., Wang, B., Wang, Y., Jiang, G., Feng, J., & Zhao, H. (2020) · Nature · doi:10.1038/s41586-020-2406-6 · Cited by 360

Navigating the Unnatural Reaction Space: Directed Evolution of Heme Proteins for Selective Carbene and Nitrene Transfer

Yang, Y., & Arnold, F. H. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.0c00591 · Cited by 359

Fragment charge difference method for estimating donor–acceptor electronic coupling: Application to DNA π-stacks

Voityuk, A. A., & Rösch, N. (2002) · The Journal of Chemical Physics · doi:10.1063/1.1502255 · Cited by 356

Exploiting and engineering hemoproteins for abiological carbene and nitrene transfer reactions

Brandenberg, O. F., Fasan, R., & Arnold, F. H. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.06.005 · Cited by 331

Electron Flow through Metalloproteins

Winkler, J. R., & Gray, H. B. (2013) · Chemical Reviews · doi:10.1021/cr4004715 · Cited by 317

Rhodamine B Equilibria

Ramette, R. W., & Sandell, E. B. (1956) · Journal of the American Chemical Society · doi:10.1021/ja01600a017 · Cited by 306

The quantum chemical cluster approach for modeling enzyme reactions

Siegbahn, P. E. M., & Himo, F. (2011) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.13 · Cited by 290

Theozymes and compuzymes: theoretical models for biological catalysis

Tantillo, D. J., Chen, J., & Houk, K. N. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80112-9 · Cited by 271

Photobiocatalysis for Abiological Transformations

Harrison, W., Huang, X., & Zhao, H. (2022) · Accounts of Chemical Research · doi:10.1021/acs.accounts.1c00719 · Cited by 267

2-Azaallyl Anions, 2-Azaallyl Cations, 2-Azaallyl Radicals, and Azomethine Ylides

Tang, S., Zhang, X., Sun, J., Niu, D., & Chruma, J. J. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00349 · Cited by 260

Electron-Tunneling Pathways in Cytochrome c

Wuttke, D. S., Bjerrum, M. J., Winkler, J. R., & Gray, H. B. (1992) · Science · doi:10.1126/science.256.5059.1007 · Cited by 235

Impact of non-proteinogenic amino acids in the discovery and development of peptide therapeutics

Ding, Y., Ting, J. P., Liu, J., Al-Azzam, S., Pandya, P., & Afshar, S. (2020) · Amino Acids · doi:10.1007/s00726-020-02890-9 · Cited by 200

Catalysis of electron transfer during activation of O 2 by the flavoprotein glucose oxidase

Roth, J. P., & Klinman, J. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252644599 · Cited by 192

Ligand Gaussian Accelerated Molecular Dynamics (LiGaMD): Characterization of Ligand Binding Thermodynamics and Kinetics

Miao, Y., Bhattarai, A., & Wang, J. (2020) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.0c00395 · Cited by 192

Stereodivergent atom-transfer radical cyclization by engineered cytochromes P450

Zhou, Q., Chin, M., Fu, Y. J., Liu, P., & Yang, Y. (2021) · Science · doi:10.1126/science.abk1603 · Cited by 190

Biosynthetic Pathways to Nonproteinogenic α-Amino Acids

Hedges, J. B., & Ryan, K. S. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00408 · Cited by 185

Engineering enzymes for noncanonical amino acid synthesis

Almhjell, P. J., Boville, C. E., & Arnold, F. H. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00665b · Cited by 183

An asymmetric sp3–sp3 cross-electrophile coupling using ‘ene’-reductases

Fu, H., Cao, J., Qiao, T., Qi, Y., Charnock, S. J., Garfinkle, S. E., & Hyster, T. K. (2022) · Nature · doi:10.1038/s41586-022-05167-1 · Cited by 183

Directed evolution of the tryptophan synthase β-subunit for stand-alone function recapitulates allosteric activation

Buller, A. R., Brinkmann‐Chen, S., Romney, D. K., Herger, M., Murciano‐Calles, J., & Arnold, F. H. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516401112 · Cited by 178

Structural basis for enzymatic photocatalysis in chlorophyll biosynthesis

Zhang, S., Heyes, D. J., Feng, L., Sun, W., Johannissen, L. O., Liu, H., Levy, C., Li, X., Yang, J. H., Yu, X., et al. (2019) · Nature · doi:10.1038/s41586-019-1685-2 · Cited by 164

Directed evolution of nonheme iron enzymes to access abiological radical-relay C(sp 3 )−H azidation

Rui, J., Zhao, Q., Huls, A. J., Soler, J., Paris, J. C., Chen, Z., Reshetnikov, V., Yang, Y., Guo, Y., Garcia‐Borràs, M., et al. (2022) · Science · doi:10.1126/science.abj2830 · Cited by 162

Quaternary Charge-Transfer Complex Enables Photoenzymatic Intermolecular Hydroalkylation of Olefins

Page, C. G., Cooper, S. J., DeHovitz, J. S., Oblinsky, D. G., Biegasiewicz, K. F., Antropow, A. H., Armbrust, K. W., Ellis, J. M., Hamann, L. G., Horn, E. J., et al. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c11462 · Cited by 151

Role of protein frame and solvent for the redox properties of azurin from Pseudomonas aeruginosa

Cascella, M., Magistrato, A., Tavernelli, I., Carloni, P., & Röthlisberger, U. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607890103 · Cited by 150

Electron flow through proteins

Gray, H. B., & Winkler, J. R. (2009) · Chemical Physics Letters · doi:10.1016/j.cplett.2009.10.051 · Cited by 145

Pyridoxal phosphate-dependent reactions in the biosynthesis of natural products

Du, Y., & Ryan, K. S. (2018) · Natural Product Reports · doi:10.1039/c8np00049b · Cited by 144

Photoinduced chemomimetic biocatalysis for enantioselective intermolecular radical conjugate addition

Huang, X., Feng, J., Cui, J., Jiang, G., Harrison, W., Zang, X., Zhou, J., Wang, B., & Zhao, H. (2022) · Nature Catalysis · doi:10.1038/s41929-022-00777-4 · Cited by 144

Reorganization Energy of Blue Copper: Effects of Temperature and Driving Force on the Rates of Electron Transfer in Ruthenium- and Osmium-Modified Azurins

Bilio, A. J. D., Hill, M. G., Bonander, N., Karlsson, G., Villahermosa, R. M., Malmström, B. G., Winkler, J. R., & Gray, H. B. (1997) · Journal of the American Chemical Society · doi:10.1021/ja971518e · Cited by 142

Using enzymes to tame nitrogen-centred radicals for enantioselective hydroamination

Ye, Y., Cao, J., Oblinsky, D. G., Verma, D., Prier, C. K., Scholes, G. D., & Hyster, T. K. (2022) · Nature Chemistry · doi:10.1038/s41557-022-01083-z · Cited by 142

Unlocking Reactivity of TrpB: A General Biocatalytic Platform for Synthesis of Tryptophan Analogues

Romney, D. K., Murciano‐Calles, J., Wehrmüller, J. E., & Arnold, F. H. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b05007 · Cited by 137

Emerging strategies for expanding the toolbox of enzymes in biocatalysis

Sandoval, B. A., & Hyster, T. K. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.12.006 · Cited by 129

Oxidation of Organotrifluoroborates via Oxone

Molander, G. A., & Cavalcanti, L. N. (2010) · The Journal of Organic Chemistry · doi:10.1021/jo102208d · Cited by 128

Semisynthetic production of unnatural L-α-amino acids by metabolic engineering of the cysteine-biosynthetic pathway

Maier, T. H. P. (2003) · Nature Biotechnology · doi:10.1038/nbt807 · Cited by 124

Dual Nickel‐ and Photoredox‐Catalyzed Enantioselective Desymmetrization of Cyclic meso‐Anhydrides

Stache, E. E., Rovis, T., & Doyle, A. G. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201700097 · Cited by 121

HPLC separation of DL-amino acids derivatized withN 2-(5-fluoro-2,4-dinitrophenyl)-L-amino acid amides

Brückner, H. J., & Keller-Hoehl, C. (1990) · Chromatographia · doi:10.1007/bf02269735 · Cited by 112

Tryptophan Synthase: Biocatalyst Extraordinaire

Watkins‐Dulaney, E. J., Straathof, S., & Arnold, F. H. (2020) · ChemBioChem · doi:10.1002/cbic.202000379 · Cited by 112

Structure and Mechanism of O-Acetylserine Sulfhydrylase

Rabeh, W. M., & Cook, P. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400001200 · Cited by 110

Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble

Buller, A. R., van Roye, P., Cahn, J. K. B., Scheele, R. A., Herger, M., & Arnold, F. H. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b03490 · Cited by 110

Synthesis of β-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase

Herger, M., van Roye, P., Romney, D. K., Brinkmann‐Chen, S., Buller, A. R., & Arnold, F. H. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b04836 · Cited by 106

A Unified Push–Pull Model for Understanding the Ring-Opening Mechanism of Rhodamine Dyes

Chi, W., Qi, Q., Lee, R., Xu, Z., & Liu, X. (2020) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.9b11673 · Cited by 101

Synthetic applications of tryptophan synthase

Phillips, R. S. (2004) · Tetrahedron Asymmetry · doi:10.1016/j.tetasy.2004.06.054 · Cited by 96

A convenient enzymatic synthesis of l-halotryptophans

Goss, R. J. M., & Newill, P. L. A. (2006) · Chemical Communications · doi:10.1039/b611929h · Cited by 89

Kinetic Isotope Effect is a Sensitive Probe of Spin State Reactivity in C−H Hydroxylation of N , N -Dimethylaniline by Cytochrome P450

Li, C., Wu, W., Kumar, D., & Shaik, S. S. (2005) · Journal of the American Chemical Society · doi:10.1021/ja055987p · Cited by 89

Suzuki-type cross-coupling of alkyl trifluoroborates with acid fluoride enabled by NHC/photoredox dual catalysis

Huang, H., Dai, Q., Leng, H., Li, Q., Yang, S.-L., Tao, Y.-M., Zhang, X., Qi, T., & Li, J. (2022) · Chemical Science · doi:10.1039/d1sc06102j · Cited by 86

Biosynthesis of Mycotoxin Fusaric Acid and Application of a PLP-Dependent Enzyme for Chemoenzymatic Synthesis of Substituted l -Pipecolic Acids

Hai, Y., Chen, M., Huang, A., & Tang, Y. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c09352 · Cited by 83

Enantioselective Carbonyl Catalysis Enabled by Chiral Aldehydes.

Wang, Q., Gu, Q., & You, S. (2019) · Angewandte Chemie · doi:10.1002/anie.201808700 · Cited by 82

Biocatalytic Access to α,α‐Dialkyl‐α‐amino Acids by a Mechanism‐Based Approach

Fesko, K., Uhl, M. K., Steinreiber, J., Gruber, K. F., & Griengl, H. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200904395 · Cited by 81

Enzymatic Pictet–Spengler Reaction: Computational Study of the Mechanism and Enantioselectivity of Norcoclaurine Synthase

Sheng, X., & Himo, F. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b04591 · Cited by 77

Does the TauD Enzyme Always Hydroxylate Alkanes, While an Analogous Synthetic Non-Heme Reagent Always Desaturates Them?

Usharani, D., Janardanan, D., & Shaik, S. S. (2010) · Journal of the American Chemical Society · doi:10.1021/ja107339h · Cited by 76

Engineered Biosynthesis of β‐Alkyl Tryptophan Analogues

Boville, C. E., Scheele, R. A., Koch, P., Brinkmann‐Chen, S., Buller, A. R., & Arnold, F. H. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201807998 · Cited by 75

Discovery and Biocatalytic Application of a PLP-Dependent Amino Acid γ‑Substitution Enzyme That Catalyzes C–C Bond Formation

Chen, M., Liu, C., & Tang, Y. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c03535 · Cited by 72

Synthesis of Unnatural Amino Acids via Suzuki Cross-Coupling of Enantiopure Vinyloxazolidine Derivatives

Sabat, M. P., & Johnson, C. R. (2000) · Organic Letters · doi:10.1021/ol005645i · Cited by 71

Bifurcating electron-transfer pathways in DNA photolyases determine the repair quantum yield

Zhang, M., Wang, L., Shu, S., Sancar, A., & Zhong, D. (2016) · Science · doi:10.1126/science.aah6071 · Cited by 63

Chiral Pyridoxal-Catalyzed Asymmetric Biomimetic Transamination of α-Keto Acids

Shi, L., Tao, C., Yang, Q., Liu, Y. E., Chen, J., Chen, J., Tian, J., Liu, F., Li, B., Du, Y., et al. (2015) · Organic Letters · doi:10.1021/acs.orglett.5b02895 · Cited by 63

Computational Mechanistic Studies Addressed to the Transimination Reaction Present in All Pyridoxal 5′-Phosphate-Requiring Enzymes

Cerqueira, N. M. F. S. A., Fernandes, P. A., & Ramos, M. J. (2011) · Journal of Chemical Theory and Computation · doi:10.1021/ct1002219 · Cited by 57

Kulokekahilide-1, a Cytotoxic Depsipeptide from the Cephalaspidean Mollusk Philinopsis speciosa

Kimura, J., Takada, Y., Inayoshi, T., Nakao, Y., Goetz, G. H., Yoshida, W. Y., & Scheuer, P. J. (2002) · The Journal of Organic Chemistry · doi:10.1021/jo010176z · Cited by 52

Emergence of oxygen‐ and pyridoxal phosphate‐dependent reactions

Hoffarth, E. R., Rothchild, K. W., & Ryan, K. S. (2020) · FEBS Journal · doi:10.1111/febs.15277 · Cited by 52

Crystallographic Snapshots of Tyrosine Phenol-lyase Show That Substrate Strain Plays a Role in C–C Bond Cleavage

Milić, D., Demidkina, T. V., Faleev, N. G., Phillips, R. S., Matković‐Čalogović, D., & Antson, A. A. (2011) · Journal of the American Chemical Society · doi:10.1021/ja203361g · Cited by 50

A Unified Synthetic Strategy to Introduce Heteroatoms via Electrochemical Functionalization of Alkyl Organoboron Reagents

Go, S. Y., Chung, H., Shin, S. J., An, S., Youn, J. H., Im, T. Y., Kim, J. Y., Chung, T. D., & Lee, H. G. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c03213 · Cited by 48

Mechanism‐Guided Computational Design of ω‐Transaminase by Reprograming of High‐Energy‐Barrier Steps

Yang, L., Zhang, K., Xu, M., Xie, Y., Meng, X., Wang, H., & Wei, D. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202212555 · Cited by 48

Palladium-catalyzed regioselective hydroboration of aryl alkenes with B 2 pin 2

Huang, J., Yan, W., Tan, C., Wu, W., & Jiang, H. (2018) · Chemical Communications · doi:10.1039/c7cc09432a · Cited by 47

Synthesis of benzylic boronates via palladium-catalyzed cross-coupling reaction of bis(pinacolato)diboron with benzylic halides

Giroux, A. (2003) · Tetrahedron Letters · doi:10.1016/s0040-4039(02)02566-2 · Cited by 46

Expanding the threonine aldolase toolbox for the asymmetric synthesis of tertiary α-amino acids

Fesko, K., Strohmeier, G. A., & Breinbauer, R. (2015) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-015-6803-y · Cited by 45

Pyridoxal-5′-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases

Frey, P. A., & Reed, G. H. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.03.005 · Cited by 39

Paper chromatographic determination of aromatic α-keto acids

Nielsen, K. H. (1963) · Journal of Chromatography A · doi:10.1016/s0021-9673(01)92338-6 · Cited by 31

Intramolecular Electron Transfer between [4Fe-4S] Clusters Studied by Proton Magnetic Resonance Spectroscopy

Kyritsis, P., Huber, J. G., Quinkal, I., Gaillard, J., & Moulis, J. (1997) · Biochemistry · doi:10.1021/bi970020m · Cited by 29

New catalytic reactions by enzyme engineering

Klaus, C., & Hammer, S. C. (2022) · Trends in Chemistry · doi:10.1016/j.trechm.2022.03.002 · Cited by 28

Mechanism of the Stereoselective Catalysis of Diels–Alderase PyrE3 Involved in Pyrroindomycin Biosynthesis

Li, B., Guan, X., Yang, S., Zou, Y., Liu, W., & Houk, K. N. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c00015 · Cited by 28

Thermodynamics of the Electron and the Proton [Erratum to document cited in CA121:19495]

Bartmess, J. E. (1995) · The Journal of Physical Chemistry · doi:10.1021/j100017a069 · Cited by 24

Antineoplastic Agents. 599. Total Synthesis of Dolastatin 16

Pettit, G. R., Smith, T. H., Arce, P. M., Flahive, E. J., Anderson, C., Chapuis, J., Xu, J., Groy, T. L., Belcher, P. E., & Macdonald, C. B. (2015) · Journal of Natural Products · doi:10.1021/np500925y · Cited by 22

One‐Pot Conversion of Amino Acids into 2,5‐Disubstituted Oxazoles: No Metals Needed

Romero‐Estudillo, I., Batchu, V. R., & Boto, A. (2014) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.201400496 · Cited by 20

Regioselective Biocatalytic Transformations Employing Transaminases and Tyrosine Phenol Lyases

Martínez‐Montero, L., Schrittwieser, J. H., & Kroutil, W. (2018) · Topics in Catalysis · doi:10.1007/s11244-018-1054-7 · Cited by 20

A shared mechanistic pathway for pyridoxal phosphate–dependent arginine oxidases

Hoffarth, E. R., Haatveit, K. C., Kuatsjah, E., MacNeil, G. A., Saroya, S., Walsby, C. J., Eltis, L. D., Houk, K. N., Garcia‐Borràs, M., & Ryan, K. S. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2012591118 · Cited by 19

Amino Acid Anhydride Hydrochlorides as Acylating Agents in Friedel-Crafts Reaction: A Practical Synthesis of l-Homophenylalanine

Mi, A., Lin, W., He, Z., Zhang, H., Zhang, X., & Jiang, Y. (2002) · Synthesis · doi:10.1055/s-2001-14563 · Cited by 17

Structural studies reveal flexible roof of active site responsible for ω-transaminase CrmG overcoming by-product inhibition

Xu, J., Tang, X., Zhu, Y., Yu, Z., Su, K., Zhang, Y., Dong, Y., Zhu, W., Zhang, C., Wu, R., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-01184-w · Cited by 13

Practical synthesis of fingolimod from diethyl acetamidomalonate

Kandagatla, B., Raju, V. V. N. K. V. P., Kumar, N. S., Reddy, G. M., Srinivas, K., Javed Iqbal, M., Bandichhor, R., & Oruganti, S. (2013) · RSC Advances · doi:10.1039/c3ra40894a · Cited by 10

Biochemical characterisation of an aldoxime-forming flavoprotein involved in 2-phenylethylglucosinolate biosynthesis in Brassica species

Oldfield, M. F., Bennett, R. N., Kiddle, G. A., Wallsgrove, R. M., & Botting, N. P. (1999) · Plant Physiology and Biochemistry · doi:10.1016/s0981-9428(99)80071-0 · Cited by 9

Stereoselective synthesis of (2S,3S)-γ-hydroxyvaline utilising an asymmetric radical hydrogen bromide addition

Easton, C. J., & Merrett, M. C. (1997) · Tetrahedron · doi:10.1016/s0040-4020(96)01045-9 · Cited by 9

New Anthranilic Acid Based Antagonists with High Affinity and Selectivity for the Human Cholecystokinin Receptor 1 (hCCK1-R)

Pavan, M. V., Lassiani, L., Berti, F., Stefancich, G., Ciogli, A., Gasparrini, F., Mennuni, L., Ferrari, F., Escrieut, C., Marco, E., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200438b · Cited by 6

Cathodic Electrochemiluminescence from Rhodamine B in Aqueous Media Using Peroxydisulfate as Co-reactant

Okada, M., Nishio, I., Takahashi, F., Tatsumi, H., & Jin, J. (2021) · Chemistry Letters · doi:10.1246/cl.210289 · Cited by 3

From nature to industry: Harnessing enzymes for biocatalysis

Buller, R., Lutz, S., Kazlauskas, R. J., Šnajdrová, R., Moore, J. C., & Bornscheuer, U. T. (2023) · Science · doi:10.1126/science.adh8615 · Cited by 759

Expanding chemistry through in vitro and in vivo biocatalysis

Kissman, E. N., Sosa, M. B., Millar, D. C., Koleski, E. J., Thevasundaram, K., & Chang, M. C. Y. (2024) · Nature · doi:10.1038/s41586-024-07506-w · Cited by 189

Stereoselective amino acid synthesis by photobiocatalytic oxidative coupling

Wang, T.-C., Mai, B. K., Zhang, Z., Bo, Z., Li, J., Liu, P., & Yang, Y. (2024) · Nature · doi:10.1038/s41586-024-07284-5 · Cited by 163

The power and pitfalls of AlphaFold2 for structure prediction beyond rigid globular proteins

Agarwal, V., & McShan, A. C. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01638-w · Cited by 155

From Ground-State to Excited-State Activation Modes: Flavin-Dependent “Ene”-Reductases Catalyzed Non-natural Radical Reactions

Fu, H., & Hyster, T. K. (2024) · Accounts of Chemical Research · doi:10.1021/acs.accounts.4c00129 · Cited by 128

Stereoselective Synthesis of Noncanonical Amino Acids Enabled by Photoredox-Pyridoxal Radical Biocatalysis

List, B., & Poje, M. M. (2023) · Synfacts · doi:10.1055/s-0042-1752035

Synergistic photoredox-pyridoxal radical biocatalysis enables synthesis of noncanonical amino acids

Wang, H., & Ye, Y. (2023) · Chem Catalysis · doi:10.1016/j.checat.2023.100753

Stereoselective amino acid synthesis by photobiocatalytic oxidative coupling

Wang, T.-C., Mai, B. K., Zhang, Z., Bo, Z., Li, J., Liu, P., & Yang, Y. (2024) · Nature · doi:10.1038/s41586-024-07284-5 · Cited by 163

Directed Evolution and Unusual Protonation Mechanism of Pyridoxal Radical C–C Coupling Enzymes for the Enantiodivergent Photobiocatalytic Synthesis of Noncanonical Amino Acids

Cheng, L., Bo, Z., Krohn-Hansen, B., & Yang, Y. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c16716 · Cited by 38

Engaging Unstabilized Alkyl Radicals with Pyridoxal Radical Biocatalysis: Enantiodivergent Synthesis of Aliphatic Non-Canonical Amino Acids

Cheng, L., Chen, J., Bo, Z., Zhang, X., Liu, P., & Yang, Y. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c16304 · Cited by 14