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  • 1
    Publication Date: 2012-12-12
    Description: 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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4046837/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4046837/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Wenjing -- Nossoni, Zahra -- Berbasova, Tetyana -- Watson, Camille T -- Yapici, Ipek -- Lee, Kin Sing Stephen -- Vasileiou, Chrysoula -- Geiger, James H -- Borhan, Babak -- R01 GM067311/GM/NIGMS NIH HHS/ -- R01-GM54082/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Dec 7;338(6112):1340-3. doi: 10.1126/science.1226135.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23224553" target="_blank"〉PubMed〈/a〉
    Keywords: Absorption ; Electrons ; Humans ; Mutagenesis ; Point Mutation ; Retinaldehyde/*analogs & derivatives/chemistry ; Retinol-Binding Proteins, Cellular/*chemistry/genetics ; Static Electricity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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