The molecular basis of spectral tuning in blue- and red-shifted flavin-binding fluorescent proteins.

ABSTRACT: Photoactive biological systems modify the optical properties of their chromophores, known as spectral tuning. Determining the molecular origin of spectral tuning is instrumental for understanding the function and developing applications of these biomolecules. Spectral tuning in flavin-binding fluorescent proteins (FbFPs), an emerging class of fluorescent reporters, is limited by their dependency on protein-bound flavins, whose structure and hence electronic properties cannot be altered by mutation. A blue-shifted variant of the plant-derived improved light, oxygen, voltage FbFP has been created by introducing a lysine within the flavin-binding pocket, but the molecular basis of this shift remains unconfirmed. We here structurally characterize the blue-shifted improved light, oxygen, voltag

SUBMITTER: Rollen K 

PROVIDER: S-EPMC8131319 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature