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We developed near-infrared (NIR) photoacoustic and fluorescence probes, as well as optogenetic tools from bacteriophytochromes, and enhanced their performance using biliverdin reductase-A knock-out model (Blvra-/-). Blvra-/- elevates endogenous heme-derived biliverdin chromophore for bacteriophytochrome-derived NIR constructs. Consequently, light-controlled transcription with IsPadC-based optogenetic tool improved up to 25-fold compared to wild-type cells, with 100-fold activation in Blvra-/- neurons.
View Article and Find Full Text PDFProbing the versatility of cytochrome c by spectroscopic means: A Laudatio on resonance Raman spectroscopy.
J Inorg Biochem
October 2024
Department of Chemistry, Drexel University, 3141 Chestnut Street, Philadelphia, PA 19104, USA. Electronic address:
Over the last 50 years resonance Raman spectroscopy has become an invaluable tool for the exploration of chromophores in biological macromolecules. Among them, heme proteins and metal complexes have attracted considerable attention. This interest results from the fact that resonance Raman spectroscopy probes the vibrational dynamics of these chromophores without direct interference from the surrounding.
View Article and Find Full Text PDFDevelopment of an miRFP680-Based Fluorescent Calcium Ion Biosensor Using End-Optimized Transposons.
ACS Sens
June 2024
Department of Chemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
The development of new or improved single fluorescent protein (FP)-based biosensors (SFPBs), particularly those with excitation and emission at near-infrared wavelengths, is important for the continued advancement of biological imaging applications. In an effort to accelerate the development of new SFPBs, we report modified transposons for the transposase-based creation of libraries of FPs randomly inserted into analyte binding domains, or vice versa. These modified transposons feature ends that are optimized to minimize the length of the linkers that connect the FP to the analyte binding domain.
View Article and Find Full Text PDFNear-infrared PAINT localization microscopy via chromophore replenishment of phytochrome-derived fluorescent tag.
Commun Biol
April 2024
SANKEN (The Institute of Scientific and Industrial Research), Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka, 567-0047, Japan.
Bacterial phytochromes are attractive molecular templates for engineering fluorescent proteins (FPs) because their near-infrared (NIR) emission significantly extends the spectral coverage of GFP-like FPs. Existing phytochrome-based FPs covalently bind heme-derived tetrapyrrole chromophores and exhibit constitutive fluorescence. Here we introduce Rep-miRFP, an NIR imaging probe derived from bacterial phytochrome, which interacts non-covalently and reversibly with biliverdin chromophore.
View Article and Find Full Text PDFRational Design of Key Enzymes to Efficiently Synthesize Phycocyanobilin in .
Biomolecules
March 2024
Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.
Phycocyanobilin (PCB) is a natural blue tetrapyrrole chromophore that is found in phycocyanin and plays an essential role in photosynthesis. Due to PCB's antioxidation, anti-inflammatory and anti-cancer properties, it has been utilized in the food, pharmaceutical and cosmetic industries. Currently, the extraction of PCB from involves complex processes, which has led to increasing interest in the biosynthesis of PCB in .
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