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Biochim Biophys Acta. 2016 May;1857(5):503-512. doi: 10.1016/j.bbabio.2015.12.002. Epub 2015 Dec 7.

First principles design of a core bioenergetic transmembrane electron-transfer protein.

Author information

1
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA.
2
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA. Electronic address: bohdana@mail.med.upenn.edu.

Abstract

Here we describe the design, Escherichia coli expression and characterization of a simplified, adaptable and functionally transparent single chain 4-α-helix transmembrane protein frame that binds multiple heme and light activatable porphyrins. Such man-made cofactor-binding oxidoreductases, designed from first principles with minimal reference to natural protein sequences, are known as maquettes. This design is an adaptable frame aiming to uncover core engineering principles governing bioenergetic transmembrane electron-transfer function and recapitulate protein archetypes proposed to represent the origins of photosynthesis. This article is part of a Special Issue entitled Biodesign for Bioenergetics--the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.

KEYWORDS:

Evolution; Intraprotein electron transfer; Light-activation; Man-made redox proteins; Maquettes; Oxidoreductase; Photosynthesis; Protein design; Respiration; Transmembrane proteins

PMID:
26672896
PMCID:
PMC4846532
DOI:
10.1016/j.bbabio.2015.12.002
[Indexed for MEDLINE]
Free PMC Article

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