Abstract
Recent advances in our understanding of the mechanism of chromophore formation in green fluorescent protein (GFP) are presented. GFP is the best-studied member of the family of GFP-like proteins, proteins that exhibit bright coloration spanning most of the visible spectrum. GFPs undergo a post-translational self-modification process that yields an intrinsic fluorophore constructed from an internal main-chain cross-link that is susceptible to air oxidation. A combination of protein X-ray crystallographic and kinetic experiments has led to the development of a mechanistic model that entails conformational pre-organization, electrophilic and base catalysis, and production of hydrogen peroxide upon protein oxidation. The process is concluded by a slow proton abstraction step from a tyrosine-derived carbon acid.
Original language | English (US) |
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Pages (from-to) | 120-127 |
Number of pages | 8 |
Journal | Accounts of chemical research |
Volume | 40 |
Issue number | 2 |
DOIs | |
State | Published - Feb 2007 |
ASJC Scopus subject areas
- General Chemistry