Channelrhodopsin C1C2: Photocycle kinetics and interactions near the central gate
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چکیده
منابع مشابه
Spectral properties and isomerisation path of retinal in C1C2 channelrhodopsin.
Structure and excited state isomerisation pathway of retinal in the channelrhodopsin chimera C1C2 have been investigated with combined quantum mechanical/molecular mechanical (QM/MM) techniques, applying CD-MS-CASPT2//CASSCF and DFT-MRCI quantum methods. The absorbing S1 state is of (1)Bu-like character, and the second excited S2 state is dominated by HOMO-LUMO double excitation with small osci...
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The light-activated microbial ion channel channelrhodopsin-2 (ChR2) is a powerful tool to study cellular processes with high spatiotemporal resolution in the emerging field of optogenetics. To customize the channel properties for optogenetic experiments, a detailed understanding of its molecular reaction mechanism is essential. Here, Glu-90, a key residue involved in the gating and selectivity ...
متن کاملMolecular Dynamics of Channelrhodopsin at the Early Stages of Channel Opening
Channelrhodopsin (ChR) is a light-gated cation channel that responds to blue light. Since ChR can be readily expressed in specific neurons to precisely control their activities by light, it has become a powerful tool in neuroscience. Although the recently solved crystal structure of a chimeric ChR, C1C2, provided the structural basis for ChR, our understanding of the molecular mechanism of ChR ...
متن کاملCharacterization of engineered channelrhodopsin variants with improved properties and kinetics.
Channelrhodopsin 2 (ChR2), a light-activated nonselective cationic channel from Chlamydomonas reinhardtii, has become a useful tool to excite neurons into which it is transfected. The other ChR from Chlamydomonas, ChR1, has attracted less attention because of its proton-selective permeability. By making chimeras of the transmembrane domains of ChR1 and ChR2, combined with site-directed mutagene...
متن کاملKinetics of proton release and uptake by channelrhodopsin-2.
Electrophysiological experiments showed that the light-activated cation channel channelrhodopsin-2 (ChR2) pumps protons in the absence of a membrane potential. We determined here the kinetics of transient pH change using a water-soluble pH-indicator. It is shown that ChR2 released protons prior to uptake with a stoichiometry of 0.3 protons per ChR2. Comparison to the photocycle kinetics reveale...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2021
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2021.03.002