Chromogenic cross-link formation in green fluorescent protein

Research output: Contribution to journalArticle

68 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)120-127
Number of pages8
JournalAccounts of Chemical Research
Volume40
Issue number2
DOIs
StatePublished - Feb 2007

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Chromogenics
Green Fluorescent Proteins
Proteins
Oxidation
Fluorophores
Chromophores
Hydrogen Peroxide
Catalysis
Tyrosine
Protons
Carbon
X rays
Kinetics
Acids
Air
Experiments

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Chromogenic cross-link formation in green fluorescent protein. / Wachter, Rebekka.

In: Accounts of Chemical Research, Vol. 40, No. 2, 02.2007, p. 120-127.

Research output: Contribution to journalArticle

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