Protein Sci, 2022, 31(3):688-700

A novel violet fluorescent protein contains a unique oxidized tyrosine as the simplest chromophore ever reported in fluorescent proteins

We describe an engineered violet fluorescent protein from the lancelet Branchiostoma floridae (bfVFP). This is the first example of a GFP-like fluorescent protein with a stable fluorescent chromophore lacking an imidazolinone ring; instead, it consists of oxidized tyrosine 68 flanked by glycine 67 and alanine 69. bfVFP contains the simplest chromophore reported in fluorescent proteins and was generated from the yellow protein lanFP10A2 by two synergetic mutations, S148H and C166I. The chromophore structure was confirmed crystallographically and by high-resolution mass spectrometry. The photophysical characteristics of bfVFP (323/430 nm, QY 0.33, and E 14,300 M cm ) make it potentially useful for multicolor experiments to expand the excitation range of available FP biomarkers and Förster resonance energy transfer with blue and cyan fluorescent protein acceptors. This article is protected by copyright. All rights reserved.

Roldán-Salgado A, Muslinkina L, Pletnev S, Pletneva N, Pletnev V, Gaytán P

IBCH: 9668
Ссылка на статью в журнале: https://onlinelibrary.wiley.com/doi/10.1002/pro.4265
Кол-во цитирований на 04.2024: 1
Данные статьи проверены модераторами 2021-12-25

Список научных проектов, где отмечена публикация

  1. - (January 6, 2019 — December 31, 2021). Pletnev V.Z.. Grant, RFBR.
  2. W-31-109-Eng-38. . Сommercial.