PMID: 11916428Mar 28, 2002Paper

The laser-induced blue state of bacteriorhodopsin: mechanistic and color regulatory roles of protein-protein interactions, protein-lipid interactions, and metal ions

Journal of the American Chemical Society
Mark B MasthayJohn T Kofron

Abstract

In this paper we characterize the mechanistic roles of the crystalline purple membrane (PM) lattice, the earliest bacteriorhodopsin (BR) photocycle intermediates, and divalent cations in the conversion of PM to laser-induced blue membrane (LIBM; lambda(max)= 605 nm) upon irradiation with intense 532 nm pulses by contrasting the photoconversion of PM with that of monomeric BR solubilized in reduced Triton X-100 detergent. Monomeric BR forms a previously unreported colorless monomer photoproduct which lacks a chromophore band in the visible region but manifests a new band centered near 360 nm similar to the 360 nm band in LIBM. The 360 nm band in both LIBM and colorless monomer originates from a Schiff base-reduced retinyl chromophore which remains covalently linked to bacterioopsin. Both the PM-->LIBM and monomer-->colorless monomer photoconversions are mediated by similar biphotonic mechanisms, indicating that the photochemistry is localized within single BR monomers and is not influenced by BR-BR interactions. The excessively large two-photon absorptivities (> or =10(6) cm(4) s molecule(-1) photon(-1)) of these photoconversions, the temporal and spectral characteristics of pulses which generate LIBM in high yield, and an actio...Continue Reading

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Citations

Dec 10, 2009·The Journal of Physical Chemistry. B·Andrei K Dioumaev, Janos K Lanyi
May 17, 2013·Journal of the Royal Society, Interface·Nicole L WagnerRobert R Birge
Mar 3, 2011·The Journal of Chemical Physics·Valentyn I ProkhorenkoLeonid S Brown
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Jun 28, 2008·Chemical Reviews·Konrad Szaciłowski
Apr 20, 2012·The Journal of Physical Chemistry. B·Daniel RhinowNorbert Hampp

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