{"id":869,"date":"2024-09-19T00:00:37","date_gmt":"2024-09-19T07:00:37","guid":{"rendered":"http:\/\/tezcan.ucsd.edu\/?page_id=869"},"modified":"2026-03-04T11:05:34","modified_gmt":"2026-03-04T19:05:34","slug":"publications-2","status":"publish","type":"page","link":"http:\/\/tezcan.ucsd.edu\/index.php\/publications-2\/","title":{"rendered":"Publications"},"content":{"rendered":"\n<p>V.H. Eng, S.M. Narehood, Y. Li, M. Gasc\u00f3n, A.M. Hoffnagle, A.A. Shiau, M. Semonis, M.T.Green, R.D Britt, F.A. Tezcan. Computational Design of a Highly Stable Dicopper Catechol Oxidase, <em>J. Am. Chem. Soc.<\/em>\u00a0(2026).\u00a0<strong><a href=\"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.5c18979?ref=article_openPDF\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>A.M. Hoffnagle, R.A. Herold, C-Y Tsai, A.A. Shiau, R.D Britt, F.A. Tezcan. <em>De Novo<\/em>&nbsp;Design of a Metalloprotein with a Synthetically Inspired Dinuclear Paddlewheel Coordination Motif, <em>J. Am. Chem. Soc.<\/em>&nbsp;(2025).&nbsp;<strong><a href=\"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.5c13813?ref=article_openPDF\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>V.H. Eng,&nbsp;M. Gasc\u00f3n,&nbsp;A. Kakkis,&nbsp;F.A. Tezcan. Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif, <em>J. Inorg. Biochem.<\/em>&nbsp;(2025).&nbsp;<strong><a href=\"https:\/\/pdf.sciencedirectassets.com\/271941\/1-s2.0-S0162013425X00118\/1-s2.0-S0162013425002855\/main.pdf?X-Amz-Security-Token=IQoJb3JpZ2luX2VjEKb%2F%2F%2F%2F%2F%2F%2F%2F%2F%2FwEaCXVzLWVhc3QtMSJHMEUCIBZ1A0XD8edTx5%2BgIG3T3DSNWrGB08TNFX%2FyTUOv7cg0AiEAzswSvmVaHFJ6JF0OuZjAfdRsHHuHazv8TNqI0QCjgycqsgUITxAFGgwwNTkwMDM1NDY4NjUiDLKfT1vQYSlJMHLXFSqPBXcZOryLcC1%2B8drntMh%2Ft4%2FTHslf95gk9PZysksEME7zSdWu7qZCdizl%2FkIPdpuyiBpWNjO0gE7MR2kiHc2Ia4zNS9eCFLWr3lu5WPSK3L1rPtekajgANFxyT0RDGHD0uppMJ0cKLtT1qadO%2B3hUaI6F6oPzjPFENyvgDUEtGw3yvrN%2FWekMSFvuyyul4yoFwbZej9FjQEaRrQAjLuzzwuMjr5TqS8D08KRrhuCvx%2FV3Y%2BriaEUppmJ7GqvI2Xkh%2FfzUKl0FfnXXGfxMar4d6kKOXVefrmfX%2Bv6Qq7vsptwLkmQN6SVIBE8837rW6PTKbgVXaW3lQVTj%2FjlcahybmzWwYs%2FrDjD2AquuT6JVZr2GtIpt5bRgYiICEBaQnOw4%2FPNBTouBF26jv3cvYmw6BuWmTIoquDnsV43Sx%2BxEu2VNnliSBC6nBBwKcQMu%2FIKjfHNX5%2FIA0KjwALC%2Fn0wfRe9xnnxt5zwBTlrgqR7OE1WJkFfrP3F1P%2F0dIbfRXTrNDTo05dB6TNjhmhsxVwpO4PaiX0nng45ABYh%2BXr4ucYks97lU871huRvE11XfR8Q0%2B5uf%2FgXd9BPiQg0t%2FoldnsgIUrCrFk7%2BjITcd9cwoqg%2F1mTd1Sfq5FUcG5SiHv7EGVMS92%2Ft7YW5MPyBOXK8vvS3rM1mkssv07Ld0yC%2BjbTm%2FE6pO678eQjEpDA%2Fy4RgX9y8O6ggxAw9UsTiKMYlOx0llFvPrDZEBzfy2REi3qC%2Bb5o2DAXvKYsI8VvZ5f%2FmStsZpEGs%2F1DYlDF7tlZUtChAA%2FuqkUuT3Mik%2FdQgR5zhGmKAlByNzvzMq%2FkvO2o84Bk5vhlryrO6sIW3HiWvpQ22hHsYm22tkF1tOxYfqPIwgeC1xwY6sQGTmDqlyDrSA3C4dm7snSYDjvO95AoTLGASN1n7RN56y7XlN5sDyLQJLi9R81jR3uRoz3PY%2F7jAAkp7Bq9C%2FFub64fxiUK6EwARwnbONC7SM4bdOOHJblK6FbreGeoqpx7wxmcbDtknZsNlgrm7nuNOOOLBrLgGBdG7%2F50O3d2JV1NsgBVK4o1We7olrN8ryl0MMs4hEsILLU53J5wFUu05rLtdyWHtyvND6%2BXLq17aPDU%3D&amp;X-Amz-Algorithm=AWS4-HMAC-SHA256&amp;X-Amz-Date=20251013T222119Z&amp;X-Amz-SignedHeaders=host&amp;X-Amz-Expires=300&amp;X-Amz-Credential=ASIAQ3PHCVTYWQJQJNON%2F20251013%2Fus-east-1%2Fs3%2Faws4_request&amp;X-Amz-Signature=d5a50b22c1ca143b0be121ac0f13476f501a1f5245bf1cb82dd717373242e560&amp;hash=8615a4f6282f2d0a01cfa04e81c53c7210c2fc1f7745e13d6eeb73a8359f3021&amp;host=68042c943591013ac2b2430a89b270f6af2c76d8dfd086a07176afe7c76c2c61&amp;pii=S0162013425002855&amp;tid=spdf-7bacd26c-9e3b-4e55-8e75-8ffa4ac0e7d0&amp;sid=c903ddc426056145c2-ba02-7331826934a2gxrqa&amp;type=client&amp;tsoh=d3d3LnNjaWVuY2VkaXJlY3QuY29t&amp;rh=d3d3LnNjaWVuY2VkaXJlY3QuY29t&amp;ua=0f165e57075650010d5650&amp;rr=98e23ab17d30f7ad&amp;cc=us\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>V. Nanda,&nbsp;J. Siess,&nbsp;B.P. Jagilinki,&nbsp;R.M. Hazen,&nbsp;S.C.L. Kamerlin,&nbsp;R. Koder,&nbsp;D. Noy,&nbsp;J. Silberg,&nbsp;F.A. Tezcan,&nbsp;R. Ulijn,&nbsp;N. Yee, P. Falkowski. On the emergence of metabolism: the evolution of proteins that powered life, <em>Phil. Trans. R. Soc. B<\/em>&nbsp;(2025).&nbsp;<strong><a href=\"https:\/\/royalsocietypublishing.org\/doi\/epdf\/10.1098\/rstb.2024.0090\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>H.T. Chiang, Z. Zhang, K. Vaddi, F.A. Tezcan, L.D. Pozzo. Efficient analysis of small-angle scattering curves for large biomolecular assemblies using Monte Carlo methods, <em>J. Appl. Cryst.&nbsp;<\/em>(2025). <strong><a href=\"https:\/\/journals.iucr.org\/j\/issues\/2025\/03\/00\/uu5014\/uu5014.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>A.M. Hoffnagle, S. Srisantitham, M. Neeley, C. Tsai, F.A.Tezcan. A&nbsp;<em>De Novo<\/em>&nbsp;Designed Protein with Versatile Metal Binding and Tunable Hydrolytic Activity, <em>Biochemistry<\/em>&nbsp;(2025).&nbsp;<strong><a href=\"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.biochem.5c00259?ref=article_openPDF\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>B.D. Cook, S.M. Narehood, K.L. McGuire, Y. Li, F.A. Tezcan, M.A. Herzik Jr. Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification, <em>Nat. Commun.<\/em>&nbsp;(2025).&nbsp;<strong><a href=\"https:\/\/www.nature.com\/articles\/s41467-025-58243-1\" data-type=\"link\" data-id=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/jacs.3c06348\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>S. Srisantitham, A.L. Walker, U. Markerl*, F.A.Tezcan*. De Novo Design of Proteins for Autocatalytic Isopeptide Bond Formation, <em>J. Am. Chem. Soc.<\/em>&nbsp;(2025).&nbsp;<strong><a href=\"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.5c03319?ref=article_openPDF\" data-type=\"link\" data-id=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/jacs.3c06348\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>Z. Zhang, H.T. Chiang, Y. Xia, N. Avakyan, R.R. Sonani, F. Wang, E.H. Egelman, J.J. De Yoreo, L.D. Pozzo, F.A. Tezcan. Design of light- and chemically responsive protein assemblies through host-guest interactions, <em>Chem<\/em> (2025). <strong><a href=\"https:\/\/www.cell.com\/chem\/fulltext\/S2451-9294(24)00652-1\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>Y. Li, J. Zhu, Z. Zhang, J. Wei, F. Wang, G. Meisl, T.P.J. Knowles, E.H. Egelman,&nbsp;F.A. Tezcan. Transforming an ATP-dependent enzyme into a dissipative, self-assembling system,<em>&nbsp;Nat. Chem. Biol.&nbsp;<\/em>(2025).&nbsp;<strong><a href=\"https:\/\/www.nature.com\/articles\/s41589-024-01811-1?fromPaywallRec=false\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>S.M. Narehood, B.D. Cook, S. Srisantitham, V.H. Eng, A.A. Shiau, K.L. McGuire, R.D. Britt, M.A. Herzik Jr,&nbsp;F.A. Tezcan. Structural basis for the conformational protection of nitrogenase from O<sub>2<\/sub>,<em>&nbsp;Nature&nbsp;<\/em>(2025).&nbsp;<strong><a href=\"https:\/\/www.nature.com\/articles\/s41586-024-08311-1\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>S. Vijayakumar*,&nbsp;R.G. Alberstein*, Z. Zhang*, Y. Lu, A. Chan, C.E. Wahl, J.S. Ha, D.E. Hunka, G.R. Boss, M.J. Sailor, F.A. Tezcan. Designed 2D protein crystals as dynamic molecular gatekeepers for a solid-state device,<em>&nbsp;Nat. Commun.<\/em>&nbsp;(2024).&nbsp;<strong><a href=\"https:\/\/www.nature.com\/articles\/s41467-024-50567-8\" data-type=\"link\" data-id=\"https:\/\/www.nature.com\/articles\/s41467-024-50567-8\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>K. Han,&nbsp;Z. Zhang, F.A. Tezcan. Spatially Patterned, Porous Protein Crystals as Multifunctional Materials,<em>&nbsp;J. Am. Chem. Soc.<\/em>&nbsp;(2023).&nbsp;<strong><a href=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/jacs.3c06348\" data-type=\"link\" data-id=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/jacs.3c06348\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>A.M. Hoffnagle, F.A. Tezcan. Atomically Accurate Design of Metalloproteins with Predefined Coordination Geometries, <em>J. Am. Chem. Soc.<\/em>&nbsp;(2023).&nbsp;<strong><a href=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/jacs.3c04047\" data-type=\"link\" data-id=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/jacs.3c04047\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>R.G. Alberstein*, J.L. Prelesnik*, E. Nakouzi, S. Zhang, J.J. De Yoreo, J. Pfaendtner, F.A. Tezcan, C.J. Mundy. Discrete Orientations of Interfacial Waters Direct Crystallization of Mica-Binding Proteins,<em>&nbsp;J. Phys. Chem. Lett.<\/em>&nbsp;(2023).&nbsp;<strong><a href=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/acs.jpclett.2c02948\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>L. Spiegelman, A. Bahn-Suh, E.T. Monta\u00f1o, L. Zhang, G.L. Hura, K.A. Patras, A. Kumar, F.A. Tezcan, V. Nizet, S.E. Tsutakawa, P. Ghosh. Strengthening of enterococcal biofilms by Esp,<em>&nbsp;PLoS pathogens<\/em>&nbsp;(2022).&nbsp;<strong><a href=\"https:\/\/journals.plos.org\/plospathogens\/article?id=10.1371\/journal.ppat.1010829\" data-type=\"link\" data-id=\"https:\/\/journals.plos.org\/plospathogens\/article?id=10.1371\/journal.ppat.1010829\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>H.L. Rutledge, M.J. Field, J. Rittle, M.T. Green, F.A. Tezcan. Role of Serine Coordination in the Structural and Functional Protection of the Nitrogenase P-Cluster,<em>&nbsp;J. Am. Chem. Soc.<\/em>&nbsp;(2022).&nbsp;<strong><a href=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/jacs.2c09480\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>T.S. Choi,&nbsp;F.A. Tezcan. Design of a Flexible, Zn-Selective Protein Scaffold that Displays Anti-Irving\u2212Williams Behavior,<em>J. Am. Chem. Soc.<\/em>&nbsp;(2022).&nbsp;<strong><a href=\"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.2c08050\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>A.M. Hoffnagle, V.H. Eng, U. Markel, F.A. Tezcan. Computationally Guided Redesign of a Heme-free Cytochrome with Native-like Structure and Stability,<em>&nbsp;Biochemistry<\/em>&nbsp;(2022).&nbsp;<strong><a href=\"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.biochem.2c00369\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>H.L. Rutledge, B.D. Cook, H.P.M. Nguyen, M.A. Herzik Jr., F.A. Tezcan. Structures of the nitrogenase complex prepared under catalytic turnover conditions,<em>&nbsp;Science&nbsp;<\/em>(2022).&nbsp;<strong><a href=\"http:\/\/www.science.org\/doi\/epdf\/10.1126\/science.abq7641\">[PDF]<\/a><\/strong>&nbsp;<strong><a href=\"http:\/\/www.science.org\/stoken\/author-tokens\/ST-649\/full\">[Free access]<\/a><\/strong><\/p>\n\n\n\n<p>K. Han*, Y. Na*, L. Zhang, F.A. Tezcan. Dynamic, Polymer-Integrated Crystals for Efficient, Reversible Protein Encapsulation,<em>&nbsp;J. Am. Chem. Soc.<\/em>&nbsp;(2022).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.2c02584\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>A. Kakkis, E. Golub, T.S. Choi,&nbsp;F.A. Tezcan. Redox- and metal-directed structural diversification in designed metalloprotein assemblies,<em>&nbsp;Chem. Commun.&nbsp;<\/em>(2022).&nbsp;<strong><a href=\"http:\/\/pubs.rsc.org\/en\/content\/articlepdf\/2022\/cc\/d2cc02440c\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>T.S. Choi,&nbsp;F.A. Tezcan. Overcoming universal restrictions on metal selectivity by protein design,<em>&nbsp;Nature&nbsp;<\/em>(2022).&nbsp;<strong><a href=\"http:\/\/www.nature.com\/articles\/s41586-022-04469-8.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J. Zhu*,&nbsp;L. Samperisi*,&nbsp;M. Kalaj, J.A. Chiong, J.B. Bailey, Z. Zhang, C. Yu, R.E. Sikma, X. Zou, S.M. Cohen, Z. Huang, F.A. Tezcan. Metal-hydrogen-pi-bonded organic frameworks,<em>&nbsp;Dalton Trans.<\/em>&nbsp;(2022).&nbsp;<strong><a href=\"http:\/\/pubs.rsc.org\/en\/content\/articlepdf\/2022\/dt\/d1dt04278e\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J. Zhu*, N. Avakyan*, A. Kakkis,&nbsp;A.M. Hoffnagle,&nbsp;K. Han,&nbsp;Y. Li,&nbsp;Z. Zhang,&nbsp;T.S. Choi,&nbsp;Y. Na,&nbsp;C. Yu, F.A. Tezcan. Protein assembly by design,<em>&nbsp;Chem. Rev.<\/em>&nbsp;(2021).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.chemrev.1c00308\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J.L. Prelesnik*, R.G. Alberstein*, S. Zhang, H. Pyles, D. Baker, J. Pfaendtner, J.J. De Yoreo, F.A. Tezcan, R.C. Remsing, C.J. Mundy. Ion-dependent protein\u2013surface interactions from intrinsic solvent response,<em>&nbsp;Proc. Natl. Acad. Sci. USA<\/em>(2021).&nbsp;<strong><a href=\"http:\/\/www.pnas.org\/content\/pnas\/archive\/118\/26\/e2025121118\/1.full.pdf?versioned=true\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>R.H. Subramanian, J. Zhu, J.B. Bailey, J.A. Chiong, Y. Li, E. Golub, F.A. Tezcan. Design of metal-mediated protein assemblies via hydroxamic acid functionalities,<em>&nbsp;Nat. Protoc.<\/em>&nbsp;(2021).&nbsp;<strong><a href=\"http:\/\/www.nature.com\/articles\/s41596-021-00535-z.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>K. Han, J.B. Bailey, L. Zhang, F.A. Tezcan. Anisotropic Dynamics and Mechanics of Macromolecular Crystals Containing Lattice-Patterned Polymer Networks,<em>&nbsp;J. Am. Chem. Soc.<\/em>&nbsp;(2020).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.0c10065\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J.B. Bailey, F.A. Tezcan. Tunable and Cooperative Thermomechanical Properties of Protein\u2013Metal\u2013Organic Frameworks,<em>J. Am. Chem. Soc.<\/em>&nbsp;(2020).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.0c07835\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>A. Kakkis, D. Gagnon, J. Esselborn, R.D. Britt, F.A. Tezcan. Metal-Templated Design of Chemically Switchable Protein Assemblies with High-Affinity Coordination Sites,<em>&nbsp;Angew. Chem. Int. Ed.<\/em>&nbsp;(2020).&nbsp;<strong><a href=\"http:\/\/onlinelibrary.wiley.com\/doi\/epdf\/10.1002\/anie.202009226\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>K.C. Bentz, K. Gnanasekaran, J.B. Bailey, S. Ayala, F.A. Tezcan, N.C. Gianneschi, S.M. Cohen. Inside polyMOFs: layered structures in polymer-based metal\u2013organic frameworks,<em>&nbsp;Chem. Sci.<\/em>&nbsp;(2020).&nbsp;<strong><a href=\"http:\/\/pubs.rsc.org\/en\/content\/articlepdf\/2020\/sc\/d0sc03651j\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>R. Subramanian, Y. Suzuki, L. Tallorin, S. Sahu, M.P. Thompson, N.C. Gianneschi, M.D. Burkart, F.A. Tezcan. Enzyme-Directed Functionalization of Designed, Two-Dimensional Protein Lattices,<em>&nbsp;Biochemistry<\/em>&nbsp;(2020).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.biochem.0c00363\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J.A. Chiong*, J. Zhu*, J.B. Bailey*, M. Kalaj, R. Subramanian, W. Xu, S.M. Cohen, F.A. Tezcan. An Exceptionally Stable Metal-Organic Framework Constructed from Chelate-based Metal-Organic Polyhedra,<em>&nbsp;J. Am. Chem. Soc.<\/em>&nbsp;(2020).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.0c01626\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>S. Zhang*, R.G. Alberstein*, J.J. De Yoreo, F.A. Tezcan. Assembly of a patchy protein into variable 2D lattices via tunable, multiscale interactions,<em>&nbsp;Nat. Commun.<\/em>&nbsp;(2020).&nbsp;<strong><a href=\"http:\/\/doi.org\/10.26434\/chemrxiv.12014925.v1\">[Preprint]<\/a>&nbsp;<a href=\"http:\/\/www.nature.com\/articles\/s41467-020-17562-1.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>H.L. Rutledge, F.A. Tezcan. Electron Transfer in Nitrogenase,<em>&nbsp;Chem. Rev.<\/em>&nbsp;(2020).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.chemrev.9b00663\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>E. Golub, R.H. Subramanian, J. Esselborn, R.G. Alberstein, J.B. Bailey, J.A. Chiong, X. Yan, T. Booth, T.S. Baker, F.A. Tezcan. Constructing protein polyhedra via orthogonal chemical interactions,<em>&nbsp;Nature&nbsp;<\/em>(2020).&nbsp;<strong><a href=\"http:\/\/www.nature.com\/articles\/s41586-019-1928-2.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>H.L Rutledge, J. Rittle, L.M. Williamson, W.A. Xu, D.M. Gagnon, F.A. Tezcan. Redox-dependent metastability of the nitrogenase P-cluster,<em>&nbsp;J. Am. Chem. Soc.&nbsp;<\/em>(2019).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.9b04555\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J. Rittle, M.J. Field, M.T. Green, F.A. Tezcan. An efficient, step-economical strategy for the design of functional metalloproteins,<em>&nbsp;Nat. Chem.&nbsp;<\/em>(2019).&nbsp;<strong><a href=\"http:\/\/www.nature.com\/articles\/s41557-019-0218-9.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>L.A. Churchfield, F.A. Tezcan. Design and Construction of Functional Supramolecular Metalloprotein Assemblies,<em>&nbsp;Acc. Chem. Res.&nbsp;<\/em>(2019).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.accounts.8b00617\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>R.H. Subramanian*, S.J. Smith*, R.G. Alberstein, J.B. Bailey, L. Zhang, G. Cardone, L. Suominen, M. Chami, H. Stahlberg, T.S. Baker, F.A. Tezcan. Self-Assembly of a Designed Nucleoprotein Architecture through Multimodal Interactions,<em>&nbsp;ACS Cent. Sci.&nbsp;<\/em>(2018).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acscentsci.8b00745\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>L.A. Churchfield, R.G. Alberstein, L.M. Williamson, F.A. Tezcan. Determining the Structural and Energetic Basis of Allostery in a&nbsp;<em>De Novo<\/em>&nbsp;Designed Metalloprotein Assembly,<em>&nbsp;J. Am. Chem. Soc.&nbsp;<\/em>(2018).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.8b05812\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>L. Zhang, J.B. Bailey, R.H. Subramanian, F.A. Tezcan. Hyperexpandable, self-healing macromolecular crystals with integrated polymer networks,<em>&nbsp;Nature&nbsp;<\/em>(2018).&nbsp;<strong><a href=\"http:\/\/www.nature.com\/articles\/s41586-018-0057-7.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>R. Alberstein, Y. Suzuki, F. Paesani, F.A. Tezcan. Engineering the entropy-driven free-energy landscape of a dynamic nanoporous protein assembly,<em>&nbsp;Nat. Chem.&nbsp;<\/em>(2018).&nbsp;<strong><a href=\"http:\/\/www.nature.com\/articles\/s41557-018-0053-4.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>W.J. Song, J. Yu, F.A. Tezcan. Importance of scaffold flexibility\/rigidity in the design and directed evolution of artificial metallo-\u03b2-lactamases,<em>&nbsp;J. Am. Chem. Soc.&nbsp;<\/em>(2017).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.7b08981\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J.B. Bailey, L. Zhang, J.A. Chiong, S. Ahn, F.A. Tezcan. Synthetic Modularity of Protein\u2013Metal\u2013Organic Frameworks,<em>&nbsp;J. Am. Chem. Soc.&nbsp;<\/em>(2017).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.7b01202\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>L.A. Churchfield, A. George, F.A. Tezcan. Repurposing proteins for new bioinorganic functions,<em>&nbsp;Essays Biochem.&nbsp;<\/em>(2017).&nbsp;<strong><a href=\"http:\/\/essays.biochemistry.org\/content\/61\/2\/245.full-text.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>S.A. Chabolla, C.W. Machan, J. Yin, E.A. Dellamary, S. Sahu, N.C. Gianneschi, M.K.Gilson, F.A. Tezcan, C.P. Kubiak. Bio-inspired CO2 reduction by a rhenium tricarbonyl bipyridine-based catalyst appended to amino acids and peptidic platforms: incorporating proton relays and hydrogen-bonding functional groups,<em>&nbsp;Farad. Discuss.&nbsp;<\/em>(2017).&nbsp;<strong><a href=\"http:\/\/pubs.rsc.org\/en\/content\/articlepdf\/2017\/fd\/c7fd00003k\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>F.E.H. Katz, X. Shi, C.P. Owens, S. Joseph, F.A. Tezcan. Determination of nucleoside triphosphatase activities from measurement of true inorganic phosphate in the presence of labile phosphate compounds,<em>&nbsp;Anal. Biochem.&nbsp;<\/em>(2017).&nbsp;<strong><a href=\"http:\/\/www.sciencedirect.com\/science\/article\/pii\/S0003269716304262\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>L.A. Churchfield, F. Medina-Morales, J.D. Brodin, A. Perez, F.A. Tezcan. De Novo Design of an Allosteric Metalloprotein Assembly with Strained Disulfide Bonds,<em>&nbsp;J. Am. Chem. Soc.&nbsp;<\/em>(2016).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.6b08458\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>C.P. Owens, F.E.H. Katz, C.H. Carter, V.F. Oswald, F.A. Tezcan. Tyrosine-coordinated P-cluster in G. diazotrophicus nitrogenase: Evidence for the importance of O-based ligands in conformationally gated electron transfer,<em>&nbsp;J. Am. Chem. Soc.&nbsp;<\/em>(2016).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.6b06783\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J.B. Bailey, R.H. Subramanian, L.A. Churchfield, F.A. Tezcan. Chapter Eleven \u2013 Metal-Directed Design of Supramolecular Protein Assemblies,<em>&nbsp;Meth. Enzym.&nbsp;<\/em>(2016).&nbsp;<strong><a href=\"http:\/\/ac.els-cdn.com\/S0076687916300441\/1-s2.0-S0076687916300441-main.pdf?_tid=46cb8720-5d88-11e6-9e6a-00000aacb35e&amp;acdnat=1470675236_80d2f16568a91ed3ac754d1cfe953362\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>F.E.H. Katz, C.P. Owens, F.A. Tezcan. Electron Transfer Reactions in Biological Nitrogen Fixation,<em>&nbsp;Isr. J. Chem.&nbsp;<\/em>(2016).&nbsp;<strong><a href=\"http:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/ijch.201600020\/epdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>Y. Suzuki, G. Cardone, D. Restrepo, P.D. Zavattieri, T.S. Baker, F.A. Tezcan. Self-assembly of coherently dynamic, auxetic, two-dimensional protein crystals,<em>&nbsp;Nature&nbsp;<\/em>(2016).&nbsp;<strong><a href=\"http:\/\/www.nature.com\/articles\/nature17633.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>S.J. Smith, R.J. Radford, R.H. Subramanian, B.R. Barnett, J.S. Figueroa, F.A. Tezcan. Tunable helicity, stability and DNA-binding properties of short peptides with hybrid metal coordination motifs,<em>&nbsp;Chem. Sci.&nbsp;<\/em>(2016).&nbsp;<strong><a href=\"http:\/\/pubs.rsc.org\/en\/content\/articlepdf\/2016\/SC\/C6SC00826G\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>C.P. Owens, F.E.H. Katz, C.H. Carter, M.A. Luca, F.A. Tezcan. Evidence for Functionally Relevant Encounter Complexes in Nitrogenase Catalysis,<em>&nbsp;J. Am. Chem. Soc.&nbsp;<\/em>(2015).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.5b08310\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>P.A. Sontz*, J.B. Bailey*, S. Ahn, F.A. Tezcan. A Metal Organic Framework with Spherical Protein Nodes: Rational Chemical Design of 3D Protein Crystals,<em>&nbsp;J. Am. Chem. Soc.<\/em>&nbsp;(2015).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.5b07463\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J.D. Brodin*, S.J. Smith*, J.R. Carr, F.A. Tezcan. Designed, Helical Protein Nanotubes with Variable Diameters from a Single Building Block,<em>&nbsp;J. Am. Chem. Soc.&nbsp;<\/em>(2015).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/jacs.5b05755\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>F.A. Tezcan, J.T. Kaiser, J.B. Howard, D.C. Rees. Structural Evidence for Asymmetrical Nucleotide Interactions in Nitrogenase,<em>&nbsp;J. Am. Chem. Soc.&nbsp;<\/em>(2014).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja511945e\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>W.J. Song, F.A. Tezcan. A designed supramolecular protein assembly with in vivo enzymatic activity,<em>&nbsp;Science&nbsp;<strong>346<\/strong><\/em>,&nbsp;1525-1528 (2014).&nbsp;<strong><a href=\"http:\/\/www.sciencemag.org\/cgi\/rapidpdf\/346\/6216\/1525?ijkey=05JKSeOkj\/OaI&amp;keytype=ref&amp;siteid=sci\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>C.W. Machan, S.A. Chabolla, J. Yin, M.K. Gilson, F.A. Tezcan, C.P. Kubiak. Supramolecular Assembly Promotes the Electrocatalytic Reduction of Carbon Dioxide by Re(I) Bipyridine Catalysts at a Lower Overpotential,&nbsp;<em>J. Am. Chem. Soc.&nbsp;<strong>136<\/strong><\/em>,&nbsp;14598-14607 (2014).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja5085282\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>S.A. Chabolla, E.A. Dellamary, C.W. Machan, F.A. Tezcan, C.P. Kubiak. Combined steric and electronic effects of positional substitution on dimethyl-bipyridine rhenium(I)tricarbonyl electrocatalysts for the reduction of CO<sub>2,<\/sub>&nbsp;<em>Inorg. Chim. Acta&nbsp;<strong>422<\/strong><\/em>, 109-113 (2014).&nbsp;<strong><a href=\"http:\/\/dx.doi.org\/10.1016\/j.ica.2014.07.007\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>P.A. Sontz*, W.J. Song*, F. A. Tezcan. Interfacial metal coordination in engineered protein and peptide assemblies,&nbsp;<em>Curr. Opin. Chem. Biol.&nbsp;<strong>19<\/strong><\/em>, 42-49 (2014).&nbsp;<strong><a href=\"http:\/\/dx.doi.org\/10.1016\/j.cbpa.2013.12.013\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>W.J. Song*, P.A. Sontz*, X.I. Ambroggio, F.A. Tezcan. Metals in protein-protein interfaces,&nbsp;<em>Annu. Rev. Biophys.&nbsp;<\/em>&nbsp;<strong><em>43<\/em><\/strong>,&nbsp;409-431&nbsp;(2014).&nbsp;<strong><a href=\"http:\/\/dx.doi.org\/10.1146\/annurev-biophys-051013-023038\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J.D. Brodin, J.R. Carr, P.A. Sontz, F.A. Tezcan. Exceptionally stable redox-active supramolecular protein assemblies with emergent properties,&nbsp;<em>Proc. Natl. Acad. Sci. USA&nbsp;<strong>111<\/strong>, 2897-2902&nbsp;<\/em>(2014).&nbsp;<strong><a href=\"http:\/\/www.pnas.org\/content\/pnas\/111\/8\/2897.full.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>A. Medina-Morales, A. Perez, J.D. Brodin, F. A. Tezcan. In Vitro and Cellular Self-Assembly of a Zn-Binding Protein Cryptand via Templated Disulfide Bonds,&nbsp;<em>J. Am. Chem. Soc.&nbsp;<strong>135<\/strong><\/em>&nbsp;12013-12022 (2013).&nbsp;<strong><a href=\"http:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/ja405318d\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>F. A. Tezcan. \u201cMetal-Directed and Templated Assembly of Protein Superstructures and Cages\u201d, in \u201cCoordination Chemistry in Protein Cages\u201d, Takafumi Ueno and Yoshi Watanabe (editors), Wiley &amp; Sons (2013).&nbsp;<strong><a href=\"http:\/\/dx.doi.org\/10.1002\/9781118571811.ch6\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>S. J. Smith*, K. Du*, R. J. Radford, F. A. Tezcan. &nbsp;Functional, metal-based cross linkers for \u03b1-helix induction in short peptides,&nbsp;<em>Chem. Sci.&nbsp;<strong>4<\/strong><\/em>, 3740-3747 (2013).&nbsp;<strong><a href=\"http:\/\/dx.doi.org\/10.1039\/C3SC50858G\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>D. J. E. Huard, K. M. Kane, F. A. Tezcan. &nbsp;Re-engineering protein interfaces yields copper-inducible ferritin cage assembly,&nbsp;<em>Nat. Chem. Biol.&nbsp;<strong>9<\/strong><\/em>, 169-176 (2013).&nbsp;<strong><a href=\"http:\/\/www.nature.com\/articles\/nchembio.1163.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>L. E. Roth and F. A. Tezcan. ATP-Uncoupled, Six-Electron Photoreduction of Hydrogen Cyanide to Methane by the Molybdenum-Iron Protein<em>, J. Am. Chem. Soc.&nbsp;<strong>134<\/strong><\/em>, 8416-8419 (2012).&nbsp;<strong><a href=\"http:\/\/dx.doi.org\/10.1021\/ja303265m\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>J.D. Brodin, X. Ambroggio, C. Tang, K. Parent, T. Baker, F.A. Tezcan. &nbsp;Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays,&nbsp;<em>Nat. Chem.&nbsp;<strong>4<\/strong><\/em>, 375-382 (2012).&nbsp;<strong><a href=\"http:\/\/www.nature.com\/articles\/nchem.1290.pdf\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>L. E. Roth and F. A. Tezcan. Light-Driven Uncoupling of Nitrogenase Catalysis from ATP Hydrolysis,&nbsp;<em>Chem. Cat. Chem.&nbsp;<strong>3<\/strong><\/em>, 1549-1555 (2011).&nbsp;<strong><a href=\"http:\/\/dx.doi.org\/10.1002\/cctc.201100216\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>E. N. Salgado, J. D. Brodin, M. M. To, F. A. Tezcan. Templated Construction of a Zn-Selective Protein Dimerization Motif<em>, Inorg. Chem.&nbsp;<strong>50<\/strong><\/em>, 6323-6329 (2011). &nbsp;<strong><a href=\"http:\/\/dx.doi.org\/10.1021\/ic200746m\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>R. J. Radford, M. Lawrenz, P. C. Nguyen, J. A. McCammon, F. A. Tezcan. Porous Protein Frameworks with Unsaturated Metal Centers in Sterically Encumbered Coordination Sites.&nbsp;<em>Chem. Commun.<\/em>,&nbsp;<strong>47<\/strong>, 313-315 (2011).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1039\/C0CC02168G\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>R. J. Radford, J. D. Brodin, E. N. Salgado, F. A. Tezcan.&nbsp; Expanding the Utility of Proteins as Platforms for Coordination Chemistry<em>, Coord. Chem. Rev.&nbsp;<\/em><strong>255<\/strong>, 790-803 (2011).&nbsp;<strong><a href=\"http:\/\/dx.doi.org\/10.1016\/j.ccr.2010.10.010\">[PDF]<\/a><\/strong><\/p>\n\n\n\n<p>L. E. Roth and F. A. Tezcan. \u201cX-ray Crystallography\u201d, in \u201cNitrogen Fixation \u2013 Methods and Protocols\u201d, M. W. Ribbe (editor), Springer\/Humana Press (2011).<\/p>\n\n\n\n<p>L. E. Roth, J. C. Nguyen, F. A. Tezcan.&nbsp; ATP- and Iron Protein-Independent Activation of Nitrogenase Catalysis by Light,&nbsp;<em>J. Am. Chem. Soc.,&nbsp;<\/em><strong>132<\/strong>, 13672-13674 (2010).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1021\/ja1071866\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>T. W. Ni, F. A. Tezcan.&nbsp; Structural Characterization of a Microperoxidase Inside a Metal-Directed Protein Cage.&nbsp;&nbsp;<em>Angew. Chem. Int. Ed.<\/em>,&nbsp;<strong>49<\/strong>, 7014-7018 (2010).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1002\/anie.201001487\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>R. J. Radford, P. C. Nguyen, F. A. Tezcan,&nbsp; Modular and Versatile Hybrid Coordination Motifs on \u03b1-Helical Protein Surfaces.&nbsp;&nbsp;<em>Inorg. Chem.,<\/em>&nbsp;<strong>49<\/strong>, 7106-7115 (2010).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1021\/ic100926g\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>J. D. Brodin, A. Medina-Morales, T. Ni, E.N. Salgado, X.I. Ambroggio, F.A. Tezcan.&nbsp; Evolution of Metal Selectivity in Templated Protein Interfaces.&nbsp;&nbsp;<em>J. Am. Chem. Soc.<\/em>,&nbsp;<strong>132<\/strong>, 8610-8617 (2010).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1021\/ja910844n\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>R. J. Radford, P. C. Nguyen, T. B. Ditri, J. S. Figureroa, F. A. Tezcan.&nbsp; Controlled Protein Dimerization through Hybrid Coordination Motifs.&nbsp;&nbsp;<em>Inorg. Chem.<\/em>,&nbsp;<strong>49<\/strong>, 4362-4369 (2010).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1021\/ic100534y\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>E. N. Salgado, R. J. Radford, F. A. Tezcan.&nbsp; Metal-Directed Protein Self-Assembly.&nbsp;&nbsp;<em>Acc. Chem. Res.<\/em>,&nbsp;<strong>43<\/strong>, 661-672 (2010).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1021\/ar900273t\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>E. N. Salgado, X.I. Ambroggio, J. D. Brodin, R. A. Lewis, B. Kuhlman, F. A. Tezcan.&nbsp; Metal Templated Design of Protein Interfaces.&nbsp;&nbsp;<em>Proc Natl Acad Sci USA<\/em>,&nbsp;<strong>107<\/strong>, 1827\u20131832 (2010).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1073\/pnas.0906852107\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>R. J. Radford, F.A. Tezcan.&nbsp; A Superprotein Triangle Driven by Nickel(II) Coordination: Exploiting Non-Natural Metal Ligands in Protein Self-Assembly.&nbsp;&nbsp;<em>J. Am. Chem. Soc.<\/em>,&nbsp;<strong>131<\/strong>, 9136-9137 (2009).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1021\/ja9000695\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>E. N. Salgado, R. A. Lewis, S. Mossin, A. L. Rheingold, F. A. Tezcan.&nbsp; Control of Protein Oligomerization Symmetry by Metal Coordination: C-2 and C-3 Symmetrical Assemblies through Cu-II and Ni-II Coordination.&nbsp;&nbsp;<em>Inorg. Chem.<\/em>,&nbsp;<strong>48<\/strong>, 2726\u20132728 (2009).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1021\/ic9001237\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>E. N. Salgado, R. A. Lewis, J. Faraone-Mennella, F. A. Tezcan.&nbsp; Metal-Mediated Self-Assembly of Protein Superstructures: Influence of Secondary Interactions on Protein Oligomerization and Aggregation.&nbsp;&nbsp;<em>J. Am. Chem. Soc.<\/em>,&nbsp;<strong>130<\/strong>, 6082\u20136084 (2008).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1021\/ja8012177\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<p>E. N. Salgado, J. Faraone-Mennella, F. A. Tezcan.&nbsp; Controlling Protein-Protein Interactions by Metal Coordination Chemistry: Assembly of a 16-Helix-Bundle Protein.&nbsp;&nbsp;<em>J. Am. Chem. Soc.<\/em>,&nbsp;<strong>129<\/strong>, 13374-13375 (2007).&nbsp;<a href=\"http:\/\/dx.doi.org\/10.1021\/ja075261o\"><strong>[PDF]<\/strong><\/a><\/p>\n\n\n\n<div style=\"height:100px\" aria-hidden=\"true\" class=\"wp-block-spacer\"><\/div>\n","protected":false},"excerpt":{"rendered":"<p>V.H. Eng, S.M. Narehood, Y. Li, M. Gasc\u00f3n, A.M. Hoffnagle, A.A. Shiau, M. Semonis, M.T.Green, R.D Britt, F.A. Tezcan. Computational Design of a Highly Stable Dicopper Catechol Oxidase, J. Am. Chem. Soc.\u00a0(2026).\u00a0[PDF] A.M. Hoffnagle, R.A. Herold, C-Y Tsai, A.A. Shiau, R.D Britt, F.A. Tezcan. De Novo&nbsp;Design of a Metalloprotein with a Synthetically Inspired Dinuclear Paddlewheel &hellip; <\/p>\n<p class=\"link-more\"><a href=\"http:\/\/tezcan.ucsd.edu\/index.php\/publications-2\/\" class=\"more-link\">Read more<span class=\"screen-reader-text\"> &#8220;Publications&#8221;<\/span><\/a><\/p>\n","protected":false},"author":2,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-869","page","type-page","status-publish","hentry"],"featured_media_urls":[],"_links":{"self":[{"href":"http:\/\/tezcan.ucsd.edu\/index.php\/wp-json\/wp\/v2\/pages\/869"}],"collection":[{"href":"http:\/\/tezcan.ucsd.edu\/index.php\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/tezcan.ucsd.edu\/index.php\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/tezcan.ucsd.edu\/index.php\/wp-json\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"http:\/\/tezcan.ucsd.edu\/index.php\/wp-json\/wp\/v2\/comments?post=869"}],"version-history":[{"count":37,"href":"http:\/\/tezcan.ucsd.edu\/index.php\/wp-json\/wp\/v2\/pages\/869\/revisions"}],"predecessor-version":[{"id":1424,"href":"http:\/\/tezcan.ucsd.edu\/index.php\/wp-json\/wp\/v2\/pages\/869\/revisions\/1424"}],"wp:attachment":[{"href":"http:\/\/tezcan.ucsd.edu\/index.php\/wp-json\/wp\/v2\/media?parent=869"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}