ArticleJournal of the American Chemical Society2010
Computational design and elaboration of a de novo heterotetrameric alpha-helical protein that selectively binds an emissive abiological (porphinato)zinc chromophore.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- De Novo Design of Parallel and Antiparallel ABiochemistry · 2025Article
- De novo design of proteins housing excitonically coupled chlorophyll special pairs.Nature chemical biology · 2024Article
- Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Corrole-protein interactions in H-NOX and HasA.RSC chemical biology · 2022Article
- Rational design of photosynthetic reaction center protein maquettes.Frontiers in molecular biosciences · 2022Article
- Designer Heme Proteins: Achieving Novel Function with Abiological Heme Analogues.Accounts of chemical research · 2021Article
- Review
- Antimicrobial activity of a porphyrin binding peptide.Peptide science (Hoboken, N.J.) · 2018Article
- De novo design of a hyperstable non-natural protein-ligand complex with sub-Å accuracy.Nature chemistry · 2017Article
- First principles design of a core bioenergetic transmembrane electron-transfer protein.Biochimica et biophysica acta · 2016Article
- Photoinduced Electron Transfer Elicits a Change in the Static Dielectric Constant of a de Novo Designed Protein.Journal of the American Chemical Society · 2016Article
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Biochemistry and theory of proton-coupled electron transfer.Chemical reviews · 2014Review
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- Elementary tetrahelical protein design for diverse oxidoreductase functions.Nature chemical biology · 2013Article
- Computational de novo design and characterization of a protein that selectively binds a highly hyperpolarizable abiological chromophore.Journal of the American Chemical Society · 2013Article
- Strategies to control the binding mode of de novo designed protein interactions.Current opinion in structural biology · 2013Review
- MAPs: a database of modular antibody parts for predicting tertiary structures and designing affinity matured antibodies.BMC bioinformatics · 2013Article
- Proteins from an unevolved library of de novo designed sequences bind a range of small molecules.ACS synthetic biology · 2012Article
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5 authors.
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Abstract
The first example of a computationally de novo designed protein that binds an emissive abiological chromophore is presented, in which a sophisticated level of cofactor discrimination is pre-engineered. This heterotetrameric, C(2)-symmetric bundle, A(His):B(Thr), uniquely binds (5,15-di[(4-carboxymethyleneoxy)phenyl]porphinato)zinc [(DPP)Zn] via histidine coordination and complementary noncovalent interactions. The A(2)B(2) heterotetrameric protein reflects ligand-directed elements of both positive and negative design, including hydrogen bonds to second-shell ligands. Experimental support for the appropriate formulation of [(DPP)Zn:A(His):B(Thr)](2) is provided by UV/visible and circular dichroism spectroscopies, size exclusion chromatography, and analytical ultracentrifugation. Time-resolved transient absorption and fluorescence spectroscopic data reveal classic excited-state singlet and triplet PZn photophysics for the A(His):B(Thr):(DPP)Zn protein (k(fluorescence) = 4 x 10(8) s(-1); tau(triplet) = 5 ms). The A(2)B(2) apoprotein has immeasurably low binding affinities for related [porphinato]metal chromophores that include a (DPP)Fe(III) cofactor and the zinc metal ion hemin derivative [(PPIX)Zn], underscoring the exquisite active-site binding discrimination realized in this computationally designed protein. Importantly, elements of design in the A(His):B(Thr) protein ensure that interactions within the tetra-alpha-helical bundle are such that only the heterotetramer is stable in solution; corresponding homomeric bundles present unfavorable ligand-binding environments and thus preclude protein structural rearrangements that could lead to binding of (porphinato)iron cofactors.
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