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Updated: Jun 14, 2026

Atomic Force Microscopy of Red-Light Photoreceptors Using PeakForce Quantitative Nanomechanical Property Mapping
Published on: October 24, 2014
Light-induced conformational changes of the chromophore and the protein in phytochromes: bacterial phytochromes as
Patrick Scheerer1, Norbert Michael, Jung Hee Park
1Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Ziegelstr. 5-9, D-10117 Berlin, Germany.
Abstract:
Recombinant phytochromes Agp1 and Agp2 from Agrobacterium tumefaciens are used as model phytochromes for biochemical and biophysical studies. In biliverdin binding phytochromes the site for covalent attachment of the chromophore lies in the N-terminal region of the protein, different from plant phytochromes. The issue which stereochemistry the chromophore adopts in the so-called Pr and Pfr forms is addressed by using a series of locked chromophores which form spectrally characteristic adducts with Agp1 and Agp2. Studies on light-induced conformational changes of Agp1 give an insight into how the intrinsic histidine kinase is modulated by light. Comparison of the crystal structure of an Agp1 fragment with other phytochrome crystal structures supports the idea that a light induced rearrangement of subunits within the homodimer modulates the activity of the kinase.
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