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| Publications [#234056] of Michael J. Therien
Papers Published
- Korendovych, IV; Senes, A; Kim, YH; Lear, JD; Fry, HC; Therien, MJ; Blasie, JK; Walker, FA; Degrado, WF, De novo design and molecular assembly of a transmembrane diporphyrin-binding protein complex.,
Journal of the American Chemical Society, vol. 132 no. 44
(November, 2010),
pp. 15516-15518 [20945900], [doi]
(last updated on 2026/01/15)
Abstract: 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.
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