Proton-Pump Mechanism in Retinal Schiff Base: On the molecular structure of the M-state

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dc.creatorDatta, Ayan
dc.creatorPati, Swapan K.
dc.date2005-07-05
dc.date.accessioned2026-07-07T05:55:18Z
dc.date.available2026-07-07T05:55:18Z
dc.descriptionTheoretical characterizations of the various intermediates in the proton pump cycle of the retinal Schiff base in the Halobacterium salinarium have been performed. Contrary to the general belief over the years that the most stable intermediate, the M-state, is a non-protonated cis-isomer, we find that the M-state is a polarized cis-isomer stabilized due to interactions of the dissociating proton with the pi-electrons. The role of proton in the pump cycle is found to be profound leading to the stabilization or in certain cases destabilization of the intermediates. We propose the chemical structure of the M-state for the first time.
dc.identifierhttps://arxiv.org/abs/physics/0507038
dc.identifierhttp://arxiv.org/abs/physics/0507038
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/87240
dc.subjectChemical Physics
dc.titleProton-Pump Mechanism in Retinal Schiff Base: On the molecular structure of the M-state
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