Chromogenic Cross-Link Formation in Green Fluorescent Protein

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• 作者：Rebekka M. Wachter
• 刊名：Accounts of Chemical Research
• 出版年：2007
• 出版时间：February 2007
• 年：2007
• 卷：40
• 期：2
• 页码：120 - 127
• 全文大小：297K
• 年卷期：v.40,no.2(February 2007)
• ISSN：1520-4898

文摘

Recent advances in our understanding of the mechanism ofchromophore formation in green fluorescent protein (GFP) arepresented. GFP is the best-studied member of the family of GFP-like proteins, proteins that exhibit bright coloration spanning mostof 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 susceptibleto air oxidation. A combination of protein X-ray crystallographicand kinetic experiments has led to the development of a mechanistic model that entails conformational pre-organization, electrophilic and base catalysis, and production of hydrogen peroxideupon protein oxidation. The process is concluded by a slow protonabstraction step from a tyrosine-derived carbon acid.