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Title: Tuning the Electronic Absorption of Protein-Embedded All-trans-Retinal

Protein-chromophore interactions are a central component of a wide variety of critical biological processes such as color vision and photosynthesis. To understand the fundamental elements that contribute to spectral tuning of a chromophore inside the protein cavity, we redesigned human cellular retinol binding protein II (hCRBPII) to fully encapsulate all-trans-retinal and form a covalent bond as a protonated Schiff base. The system, using rational mutagenesis designed to alter the electrostatic environment within the binding pocket of the host protein, enabled regulation of the absorption maximum of the pigment in the range of 425 to 644 nanometers. Moreover, with only nine point mutations, the hCRBPII mutants induced a systematic shift in the absorption profile of all-trans-retinal of more than 200 nanometers across the visible spectrum.
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  1. Michigan State Univ., East Lansing, MI (United States)
Publication Date:
OSTI Identifier:
DOE Contract Number:
FG02-06ER15822; W-31-109-ENG-38
Resource Type:
Journal Article
Resource Relation:
Journal Name: Science (New York, N.Y., Online); Journal Volume: 338; Journal Issue: 12, 2012
Research Org:
Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States