Journal
SCIENCE
Volume 338, Issue 6112, Pages 1340-1343Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1226135
Keywords
-
Categories
Funding
- NIH [R01-GM54082]
- U.S. Department of Energy (DOE), Office of Science, Basic Energy Sciences, Chemical Sciences, Geosciences and Biosciences Division [DE-FG02-06ER15822]
- DOE Office of Energy Research [W-31-109-ENG-38]
- DOE, Office of Science, Basic Energy Sciences [W-31-109-ENG-38]
Ask authors/readers for more resources
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. This 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. 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available