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Bruce R. Lichtenstein, Ph.D.

Affiliations: 
2012-2013 Chemical Biology University of Oxford, Oxford, United Kingdom 
 2013-2012 Biochemistry and Biophysics University of Pennsylvania, Philadelphia, PA, United States 
 2013-2016 Protein Engineering Max Planck Institute for Developmental Biology, Tübingen, Tübingen, Baden-Württemberg, Germany 
 2016-2018 Biochemistry University of Bayreuth 
 2019- Centre for Enzyme Engineering University of Portsmouth, Portsmouth, England, United Kingdom 
Area:
oxidation-reduction in biological systems, protein design, enzyme engineering, directed evolution, chemical biology
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"Bruce Lichtenstein"
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Parents

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Robert S. Paley research assistant 2001-2002 Swarthmore
P. Leslie Dutton grad student 2010 Penn
 (A new approach to understanding biological control of quinone electrochemistry.)
Benjamin G. Davis post-doc 2012-2013 Oxford
Birte Hocker post-doc 2013-2018 University of Bayreuth

Children

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Collaborators

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Jeffery G. Saven collaborator Penn
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Publications

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Avilan L, Lichtenstein BR, Koenig G, et al. (2023) Concentration-dependent inhibition of mesophilic PETases on poly(ethylene terephthalate) can be eliminated by enzyme engineering. Chemsuschem. e202202277
Lichtenstein BR, Höcker B. (2018) Engineering an AB Protein Carrier. Scientific Reports. 8: 12643
Lichtenstein BR, Bialas C, Cerda JF, et al. (2015) Designing Light-Activated Charge-Separating Proteins with a Naphthoquinone Amino Acid. Angewandte Chemie (International Ed. in English). 54: 13626-9
Anderson JL, Armstrong CT, Kodali G, et al. (2014) Constructing a man-made c-type cytochrome maquette in vivo: electron transfer, oxygen transport and conversion to a photoactive light harvesting maquette. Chemical Science (Royal Society of Chemistry : 2010). 5: 507-514
Farid TA, Kodali G, Solomon LA, et al. (2014) Erratum: Corrigendum: Elementary tetrahelical protein design for diverse oxidoreductase functions Nature Chemical Biology. 10: 164-164
Farid TA, Kodali G, Solomon LA, et al. (2013) Elementary tetrahelical protein design for diverse oxidoreductase functions. Nature Chemical Biology. 9: 826-33
Kodali G, Solomon LA, Englander MT, et al. (2013) Design and Engineering of Protein Platforms for Multiple Functions Biophysical Journal. 104: 661a
Raju G, Capo J, Lichtenstein BR, et al. (2012) Manipulating Reduction Potentials in an Artificial Safranin Cofactor. Tetrahedron Letters. 53: 1201-1203
Lichtenstein BR, Farid TA, Kodali G, et al. (2012) Engineering oxidoreductases: maquette proteins designed from scratch. Biochemical Society Transactions. 40: 561-6
Lichtenstein BR, Moorman VR, Cerda JF, et al. (2012) Electrochemical and structural coupling of the naphthoquinone amino acid. Chemical Communications (Cambridge, England). 48: 1997-9
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