De novo design and molecular assembly of a transmembrane diporphyrin-binding protein complex.
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The de novo design of membrane proteins remains difficult despite recent advances in understanding the factors that drive membrane protein folding and association. We have designed a membrane protein PRIME (PoRphyrins In MEmbrane) that positions two non-natural iron diphenylporphyrins (Fe(III)DPP's) sufficiently close to provide a multicentered pathway for transmembrane electron transfer. Computational methods previously used for the design of multiporphyrin water-soluble helical proteins were extended to this membrane target. Four helices were arranged in a D(2)-symmetrical bundle to bind two Fe(II/III) diphenylporphyrins in a bis-His geometry further stabilized by second-shell hydrogen bonds. UV-vis absorbance, CD spectroscopy, analytical ultracentrifugation, redox potentiometry, and EPR demonstrate that PRIME binds the cofactor with high affinity and specificity in the expected geometry.
Published Version (Please cite this version)10.1021/ja107487b
Publication InfoKorendovych, Ivan V; Senes, Alessandro; Kim, Yong Ho; Lear, James D; Fry, H Christopher; Therien, Michael J; ... Degrado, William F (2010). De novo design and molecular assembly of a transmembrane diporphyrin-binding protein complex. J Am Chem Soc, 132(44). pp. 15516-15518. 10.1021/ja107487b. Retrieved from https://hdl.handle.net/10161/4046.
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William R. Kenan, Jr. Distinguished Professor of Chemistry
Our research involves the synthesis of compounds, supramolecular assemblies, nano-scale objects, and electronic materials with unusual ground-and excited-state characteristics, and interrogating these structures using state-of-the-art transient optical, spectroscopic, photophysical, and electrochemical methods. Over chemical dimensions that span molecules to materials, we probe experimental and theoretical aspects of charge migration reactions and ultrafast electron transfer processes. Insights