BphP1/PpsR2

Photoreceptor BphP1
Binding partner PpsR2
Cofactor Biliverdin
Source organism Rhodopseudomonas palustris
Mode of action heterodimerization
Excitation wavelength 760 nm
Reversion wavelength 640 nm (faster), dark (slower)
Excitation time seconds
Reversion time seconds
Crystal structure of a point mutated (C20S) BphP1 photoreceptor, without PpsR2. Note: no wild type structure available at the moment. (PDB ID: 4XTQ)

BphP1/PpsR2-derived switches:

Related original publications

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  1. Creating Red Light-Switchable Protein Dimerization Systems as Genetically Encoded Actuators with High Specificity. ACS Synth Biol, 2020
  2. Biliverdin reductase-A deficiency brighten and sensitize biliverdin-binding chromoproteins. Cell Struct Funct, 2020
  3. Near-infrared light-controlled systems for gene transcription regulation, protein targeting and spectral multiplexing. Nat Protoc, 2018
  4. Engineering an E. coli Near-Infrared Light Sensor. ACS Synth Biol, 2017
  5. Near-infrared optogenetic pair for protein regulation and spectral multiplexing. Nat Chem Biol, 2017
  6. A bacterial phytochrome-based optogenetic system controllable with near-infrared light. Nat Methods, 2016
  7. Multiscale photoacoustic tomography using reversibly switchable bacterial phytochrome as a near-infrared photochromic probe. Nat Methods, 2015
  8. Particle aggregation in photosynthetic membranes of the blue-green alga Anacystis nidulans. Biochim Biophys Acta, 1978