Chromophore Formation in DsRed Occurs by a Branched Pathway

Like GFP, the fluorescent protein DsRed has a chromophore that forms autocatalytically within the folded protein, but the mechanism of DsRed chromophore formation has been unclear. It was proposed that an initial oxidation generates a green chromophore, and that a final oxidation yields the red chro...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2010-06, Vol.132 (24), p.8496-8505
Main Authors: Strack, Rita L, Strongin, Daniel E, Mets, Laurens, Glick, Benjamin S, Keenan, Robert J
Format: Article
Language:English
Subjects:
Color
Hydrogen Peroxide - chemistry
Kinetics
Luminescent Proteins - chemistry
Luminescent Proteins - genetics
Luminescent Proteins - metabolism
Models, Chemical
Mutation
Oxidation-Reduction
Oxygen - chemistry
Solubility
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Summary:Like GFP, the fluorescent protein DsRed has a chromophore that forms autocatalytically within the folded protein, but the mechanism of DsRed chromophore formation has been unclear. It was proposed that an initial oxidation generates a green chromophore, and that a final oxidation yields the red chromophore. However, this model does not adequately explain why a mature DsRed sample contains a mixture of green and red chromophores. We present evidence that the maturation pathway for DsRed branches upstream of chromophore formation. After an initial oxidation step, a final oxidation to form the acylimine of the red chromophore is in kinetic competition with a dehydration to form the green chromophore. This scheme explains why green and red chromophores are alternative end points of the maturation pathway.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja1030084