Division of Chemistry and Chemical Engineering 210-41
California Institute of Technology
Pasadena, California 91125 USA
Date of birth 25 July 1956
Place Pittsburgh, Pennsylvania, United States of America (America)
Nomination 08 October 2019
Field Chemical Engineering, Bioengineering, Biochemistry, Chemistry
Title Linus Pauling Professor of Chemical Engineering, Bioengineering and Biochemistry, Nobel laureate in Chemistry, 2018
Most important awards, prizes and academies
Membership of Professional Societies: Royal Academy of Engineering (UK); American Philosophical Society; American Academy of Arts and Sciences; National Academy of Sciences (USA); National Academy of Medicine (USA); National Academy of Engineering (USA); American Chemical Society; American Institute of Chemical Engineers; Fellow, American Association for the Advancement of Science Fellow, American Society for Microbiology; Fellow, American Institute for Medical and Biological Engineering. Honours (Citations, Awards, etc.) 2019 Honorary Doctorate, Technical University of Denmark; 2019 SynBioBeta Pioneer in Synthetic Biology Award; 2019 Bower Award for Advancement in Science, Franklin Institute; 2018 Nobel Prize in Chemistry, Royal Swedish Academy of Sciences; 2018 International Fellow, UK Royal Academy of Engineering; 2018 American Philosophical Society; 2017 Society of Women Engineers Lifetime Achievement Award; 2017 Margaret H Rousseau Pioneer Award, AIChE; 2017 Rotary Humanitarian Heroes of Science & Technology Award; 2017 Robert Fletcher Award and Honorary Doctorate, Dartmouth University; 2017 National Academy of Sciences Sackler Prize in Convergence Research; 2016 Millennium Technology Prize, Technology Academy Finland; 2016 Honorary Doctorate, University of Chicago; 2015 Honorary Doctorate, ETH Zurich; 2015 Elmer Gaden Award, Biotechnology & Bioengineering; 2014 Fellow, National Academy of Inventors; 2014 Golden Plate Award, Academy of Achievement; 2014 US National Inventors Hall of Fame; 2013 Eni Prize in Renewable and Nonconventional Energy; 2013 Doctorate honoris causa, Stockholm University; 2011 US National Medal of Technology and Innovation; 2011 Charles Stark Draper Prize of the National Academy of Engineering; 2011 Fellow, American Academy of Arts and Sciences; 2009 Fellow, American Association for the Advancement of Science; 2009 Fellow, American Academy of Microbiology; 2008 Elected to the National Academy of Sciences; 2008 Technology Review TR10 (10 emerging technologies for 2008); 2007 Enzyme Engineering Award, Engineering Foundation; 2007 FASEB Excellence in Science Award; 2005 Garvin-Olin Medal, American Chemical Society; 2005 Food, Pharmaceuticals, and Bioengineering Division Award, AIChE 2004 Elected to the Institute of Medicine of the National Academies; 2003 Carothers Award, American Chemical Society Delaware Division; 2003 David Perlman Lecture Award, American Chemical Society, BIOT; 2001 Fellow, American institute for Medical and Biological Engineering; 2000 Elected to the National Academy of Engineering; 2000 Professional Progress Award, American Institute of Chemical Engineers; 1995 American Institute of Chemical Engineers, Separations Division Graduate Research; Paper Award (with V. Sundaresan); 1989 NSF Presidential Young Investigator Award; 1989 David and Lucile Packard Fellowship in Science and Engineering; 1989 Whitaker Foundation Investigator; 1988 Office of Naval Research Young Investigator Award (Molecular Biology) 1979 Phi Beta Kappa, Tau Beta Pi.
Summary of scientific research
We study Nature’s powerful biological design process, evolution. We use it to optimize existing proteins and create new ones, thereby circumventing our profound ignorance of how sequence encodes function. With ‘directed evolution’ and chemical understanding, we have generated whole new enzyme families that catalyze synthetically important chemical reactions not known in biology. These new capabilities increase the scope of molecules and materials we can build using biological systems and move us closer to a sustainable world where chemical synthesis can be fully programmed in DNA.
Selected Peer-reviewed Publications
C.N. Bedbrook, K. Yang, J.E. Robinson, V. Gradinaru, F.H. Arnold. “Machine Learning-Guided Channelrhodopsin Engineering Enables Minimally-Invasive Optogenetics. Nature Methods, published online October 14, 2019: https://www.nature.com/articles/s41592-019-0583-8; I. Cho, Z.-J. Jia, F.H. Arnold “Site-Selective Enzymatic C-H Amidation for Synthesis of Diverse Lactams.” Science 364, 575-578 (2019). doi: 10.1126/science.aaw9068; Z. Wu, S.B.J. Kan, R.D. Lewis, B.J. Wittmann, F.H. Arnold “Machine-Learning-Assisted Directed Protein Evolution with Combinatorial Libraries.” Proceedings of the National Academy of Sciences 116(18), 8852-8858 (2019). doi: 10.1073/pnas.1901979116; R.K. Zhang, K. Chen, X, Huang, L. Wohlschlager, H. Renata, F.H. Arnold. "Enzymatic Assembly of Carbon-Carbon Bonds via Iron-Catalysed sp3 C-H Functionalization" Nature 565, 67-72 (2019). doi: 10.1038/s41586-018-0808-5; K. Chen, X. Huang, S.B.J. Kan, R.K. Zhang, F.H. Arnold, “Enzymatic Construction of Highly Strained Carbocyles.” Science 360, 71-75 (2018). doi: 10.1126/science.aar4239; S.B.J. Kan, X. Huang, Y. Gumulya, K. Chen, F.H. Arnold, “Genetically Programmed Chiral Organoborane Synthesis.” Nature 552, 132-136 (2017). doi: 10.1038/nature24996; C.K. Prier, R.K. Zhang, A.R. Buller, S. Brinkmann-Chen, F.H. Arnold, “Enantioselective, Intermolecular Benzylic C-H Amination Catalyzed by an Engineered Iron-Haem Enzyme.” Nature Chemistry 9, 629-634 (2017). doi:10.1038/NCHEM.2783; S.B.J. Kan, R.D. Lewis, K. Chen, F.H. Arnold. “Directed Evolution of Cytochrome c for Carbon–Silicon Bond Formation: Bringing Silicon to Life.” Science 354, 1048-1051 (2016). doi:10.1126/science.aah6219; J.K.B. Cahn, S. Brinkmann-Chen, A.R. Buller, F.H. Arnold, “Artificial Domain Duplication Replicates Evolutionary History of Ketol-Acid Reductoisomerases.” Protein Science 25, 1241-1248 (2016). doi:10.1002/pro.2852; A.R. Buller, S. Brinkmann-Chen, D.K. Romney, M. Herger, J. Murciano-Calles, F.H. Arnold, “Directed Evolution of the Tryptophan Synthase b-Subunit for Stand-Alone Function Recapitulates Allosteric Activation.” Proceedings of the National Academy of Sciences USA 112, 14599-14604 (2015). doi:10.1073/pnas.1516401112; J.A. McIntosh, P.S. Coelho, C.C. Farwell, Z.J. Wang, J.C. Lewis, T.R. Brown, F.H. Arnold, “Enantioselective Intramolecular C-H Amination Catalyzed by Engineered Cytochrome P450 Enzymes in vitro and in vivo.” Angewandte Chemie International Edition 52, 9309-9312 (2013); P. S. Coelho, E. M. Brustad, A. Kannan, F.H. Arnold. “Olefin Cyclopropanation via Carbene Transfer Catalyzed by Engineered Cytochrome P450 Enzymes.” Science 339, 307-310 (2013); P.A. Romero, A. Krause, F.H. Arnold, “Navigating the Protein Fitness Landscape with Gaussian Processes.” Proc. Natl. Acad. Sci. USA 110(3), E193-E201 (2012); R. Fasan, Y. T. Meharenna, C.D. Snow, T.L. Poulos, F.H. Arnold, “Evolutionary History of a Specialized P450 Propane Monooxygenase.” J. Mol. Biol. 383(5): 1069-1080 (2008); J. D. Bloom, S. Labthavikul, C. R. Otey, F. H. Arnold, “Protein Stability Promotes Evolvability.” Proceedings of the National Academy of Sciences 103, 5869-5874 (2006); D.A. Drummond, J.D. Bloom, C. Adami, C. Wilke, F.H. Arnold, “Why Highly Expressed Proteins Evolve Slowly.” Proc. Natl. Acad. Sci., 102, 14338-14343 (2005); D.A. Drummond, J.J. Silberg, M.M. Meyer, C.O. Wilke, F.H. Arnold, “On the Conservative Nature of Intragenic Recombination.” Proc. Natl. Acad. Sci. 102, 5380-5385 (2005); J.D. Bloom, J.J. Silberg, C.O. Wilke, D.A. Drummond, C. Adami, F.H. Arnold, “Thermodynamic Prediction of Protein Neutrality.” Proc. Natl. Acad. Sci. 102, 606-611 (2005); S. Basu, Y. Gerchman, C.H. Collins, F.H. Arnold, R. Weiss, “A Synthetic Multicellular System for Programmed Pattern Formation.” Nature 434, 1130-1134 (2005); L. You, R. S. Cox III, R. Weiss, F. H. Arnold, “Programmed Population Control by Cell-Cell Communication and Regulated Killing.” Nature 428, 868-871 (2004); Y. Yokobayashi, R. Weiss, F.H. Arnold, “Directed Evolution of a Genetic Circuit,” Proceedings of the National Academy of Sciences USA 99, 16587-16591 (2002); C.A. Voigt, C. Martinez, Z.-G. Wang, S. L. Mayo, F.H. Arnold, “Protein Building Blocks Preserved by Recombination.” Nature Structural Biology 9, 553-558 (2002); T. Thorsen, R.W. Roberts, F.H. Arnold, S.R. Quake, “Dynamic Pattern Formation in a Vesicle-Generating Microfluidic Device,” Physical Review Letters 86, 4163-4166 (2001); C. Schmidt-Dannert, D. Umeno, F.H. Arnold, “Molecular Breeding of Carotenoid Biosynthetic Pathways.” Nature Biotechnology 18, 750-753 (2000); B. Spiller, A. Gershenson, F.H. Arnold, R.C. Stevens, “A Structural View of Evolutionary Divergence.” Proceedings of the National Academy of Sciences USA 96, 12305-12310 (1999); L. Giver, A. Gershenson, P.-O. Freskgard, F.H. Arnold, “Directed Evolution of a Thermostable Esterase.” Proc. Natl. Acad. Sci. USA 95, 12809-12813 (1998); H. Zhao, L. Giver, Z. Shao, J.A. Affholter, F.H. Arnold, "Molecular Evolution by Staggered Extension Process (StEP) in vitro Recombination." Nature Biotechnology 16, 258-262 (1998); F.H. Arnold, "Design by Directed Evolution." Accounts of Chemical Research 31, 125-131 (1998); J.C. Moore, F.H. Arnold, "Directed Evolution of a para-Nitrobenzyl Esterase for Aqueous-Organic Solvents." Nature Biotechnology 14, 458-467 (1996); K. Chen, F.H. Arnold, "Tuning the Activity of an Enzyme for Unusual Environments: Sequential Random Mutagenesis of Subtilisin E for Catalysis in Dimethylformamide." Proc. Natl. Acad. Sci. USA 90, 5618-5622 (1993). Selected Book Chapters, Reviews, Commentaries, Editorials: F.H. Arnold, “Innovation by Evolution: Bringing New Chemistry to Life (Nobel Lecture).” Angewandte Chemie Int. Ed. 58, 2-9 (2019). doi: 10.1002/anie.201907729; F. H. Arnold, “The Library of Maynard-Smith: My Search for Meaning in the Protein Universe"; J. D. Bloom, F. H. Arnold, “In the Light of Directed Evolution: Pathways of Adaptive Protein Evolution.” PNAS 106 (suppl. 1), 9995-10000 (2009); F.H. Arnold, P.L. Wintrode, K. Miyazaki, A. Gershenson,“ How Enzymes Adapt: Lessons from Laboratory Evolution.” Trends in Biochemical Sciences 26, 100-106 (2001); F.H. Arnold, "Directed Evolution: Creating Biocatalysts for the Future," Chemical Engineering Science 51, 5091-5102 (1996).
Division of Chemistry and Chemical Engineering 210-41