A5015284437- Photosynthetic Processes and Mechanisms
- Photoreceptor and optogenetics research
- Spectroscopy and Quantum Chemical Studies
- Light effects on plants
- Molecular spectroscopy and chirality
- Protein Structure and Dynamics
- Advanced NMR Techniques and Applications
- Origins and Evolution of Life
Hebrew University of Jerusalem
2018-2023
Migal - Galilee Technology Center
2020-2023
Western Galilee Hospital
2021
Electrostatic interactions with the protein control spectral tuning of chlorophyll.
Cyanobacteriochromes are bistable photoreceptor proteins with desirable photochemical properties for biotechnological applications, such as optogenetics or fluorescence microscopy. Here, we investigate Slr1393-g3, a cyanobacteriochrome that reversibly photoswitches between red-absorbing (Pr) and green-absorbing (Pg) form. We applied advanced IR spectroscopic methods to track the sequence of intermediates during photocycle over many orders magnitude in time. In conversion from Pg Pr, have...
Photosystem II reaction centers extract electrons from water, providing the basis of oxygenic life on earth. Among light-sensitive pigments center, a central chlorophyll dimer, known as special pair, so far has escaped complete theoretical characterization its excited state properties. The close proximity pair gives rise to short-range effects that comprise coupling between local and charge transfer (CT) states well other intermolecular quantum effects. Using multiscale simulation...
Cyanobacteriochromes are bi-stable photoreceptor proteins with desirable photochemical properties for biotechnological applications such as optogenetics or fluorescence microscopy. Here, we investigated Slr1393-g3, a cyanobacteriochrome that reversibly photo-switches between red-absorbing (Pr) and green-absorbing (Pg) form. We applied advanced IR spectroscopic methods to track the sequence of intermediates during photocycle over many orders in magnitude time. In conversion from Pg Pr, have...
Simple optical spectroscopy measurements, namely circular dichroism (CD) and absorption spectra of interacting pigments, can be used for deriving details their molecular geometry. Unlike X-ray crystallography NMR that provide highly detailed structural information but consume time resources, spectroscopic measurements valuable on local interactions are fast, easy to perform. Unfortunately, may extracted from only upon solving an ill-defined inverse-problem (spectrum → structure). In this...
In photosynthetic complexes, tuning of chlorophyll light-absorption spectra by the protein environment is crucial to their efficiency and robustness. Water Soluble Chlorophyll-binding Proteins from Brassicaceae (WSCPs) are useful for studying spectral mechanisms due symmetric homotetramer structure, ability rigorously modify chlorophyll’s surroundings, availability crystal structures. Here, we present a rigorous analysis based on hybrid Quantum Mechanics Molecular simulations with...
Abstract The molecular structure of mBDFP, a far‐red fluorescent protein (FPs) derived from an allophycocyanin homolog was resolved to 2.52 Å. Its biliverdin chromophore found be attached the in unusual way that never observed natural phycobiliproteins, and only once sub‐population artificial bacteriophytochrome‐derived FPs. One biliverdin's vinyl groups had two cysteine residues covalently bound its carbon atoms. This reduces conjugation length π‐electron system, which shifts absorption...
In photosynthetic complexes, tuning of chlorophyll light-absorption spectra by the protein environment is crucial to their efficiency and robustness. Water Soluble Chlorophyll-binding Proteins from <i>Brassicaceae</i> (WSCPs) are useful for studying spectral mechanisms due symmetric homotetramer structure, ability rigorously modify chlorophyll’s surroundings, availability crystal structures. Here, we present a rigorous analysis based on hybrid Quantum Mechanics Molecular...