Chromogenic cross-link formation in green fluorescent protein.
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.
Wachter
Rebekka M
RM
Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona 85287, USA. RWachter@asu.edu
D000143:Acids / Q000737:chemistry; D000388:Air; D002244:Carbon / Q000737:chemistry; D002384:Catalysis; D003432:Cross-Linking Reagents / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D049452:Green Fluorescent Proteins / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D006861:Hydrogen Peroxide / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D049408:Luminescent Agents / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D011522:Protons; D014443:Tyrosine / Q000737:chemistry
D000143:Acids; D003432:Cross-Linking Reagents; D049408:Luminescent Agents; D011522:Protons; D049452:Green Fluorescent Proteins; D014443:Tyrosine; D002244:Carbon; D006861:Hydrogen Peroxide