Search Results - "Hegemann, P"

Conversion of a light-driven proton pump into a light-gated ion channel by Vogt, A., Guo, Y., Tsunoda, S. P., Kateriya, S., Elstner, M., Hegemann, P.

“…Interest in microbial rhodopsins with ion pumping activity has been revitalized in the context of optogenetics, where light-driven ion pumps are used for cell…”
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Channelrhodopsins: directly light-gated cation channels by Nagel, G, Szellas, T, Kateriya, S, Adeishvili, N, Hegemann, P, Bamberg, E

“…Phototaxis and photophobic responses of green algae are mediated by rhodopsins with microbial type chromophores, i.e. all-trans-retinal in the ground state…”
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Synthetic retinal analogues modify the spectral and kinetic characteristics of microbial rhodopsin optogenetic tools by AzimiHashemi, N., Erbguth, K., Vogt, A., Riemensperger, T., Rauch, E., Woodmansee, D., Nagpal, J., Brauner, M., Sheves, M., Fiala, A., Kattner, L., Trauner, D., Hegemann, P., Gottschalk, A., Liewald, J. F.

“…Optogenetic tools have become indispensable in neuroscience to stimulate or inhibit excitable cells by light. Channelrhodopsin-2 (ChR2) variants have been…”
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Photo-dynamics of BLUF domain containing adenylyl cyclase NgPAC3 from the amoeboflagellate Naegleria gruberi NEG-M strain by Penzkofer, A., Tanwar, M., Veetil, S.K., Kateriya, S., Stierl, M., Hegemann, P.

“…•Photo-activated adenylyl cyclase NgPAC3 from Naegleria gruberi NEG-M was expressed.•Photo-cycle dynamics of BLUF domain in NgPAC3 protein was studied.•Flavin…”
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Photo-dynamics of the BLUF domain containing soluble adenylate cyclase (nPAC) from the amoeboflagellate Naegleria gruberi NEG-M strain by Penzkofer, A., Stierl, M., Hegemann, P., Kateriya, Suneel

“…The photoactivated adenylyl cyclase (nPAC) from Naegleria gruberi was expressed heterologously in Escherichia coli and its photo-cycling dynamics was studied…”
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pH dependence of the absorption and emission behaviour of riboflavin in aqueous solution by Drössler, P., Holzer, W., Penzkofer, A., Hegemann, P.

“…The absorption and fluorescence behaviour of riboflavin is investigated in aqueous solution over a wide range of pH values from pH=−1.1 to pH=13.4. Absorption…”
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Photo-induced degradation of some flavins in aqueous solution by Holzer, W., Shirdel, J., Zirak, P., Penzkofer, A., Hegemann, P., Deutzmann, R., Hochmuth, E.

“…The blue-light induced photo-degradation of FMN, FAD, riboflavin, lumiflavin, and lumichrome in aqueous solution at pH 8 is studied by measurement of…”
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Thermal protein unfolding in photo-activated adenylate cyclase nano-clusters from the amoeboflagellate Naegleria gruberi NEG-M strain by Penzkofer, A., Stierl, M., Hegemann, P., Kateriya, S.

“…[Display omitted] ► Apparent melting temperature of 60 °C is determined by static light scattering measurement. ► Temporal development of protein unfolding is…”
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Concept for a single-shot mid-infrared spectrometer using synchrotron radiation by Schade, U., Ritter, E., Hegemann, P., Aziz, E.F., Hofmann, K.P.

“…Several attempts have been made to extend time-resolved mid infrared spectroscopy to higher time resolution. Such methods are either limited to specific…”
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Vibrational Spectroscopy of an Algal Phot-LOV1 Domain Probes the Molecular Changes Associated with Blue-Light Reception by Ataka, K., Hegemann, P., Heberle, J.

“…The LOV1 domain of the blue light Phot1-receptor (phototropin homolog) from Chlamydomonas reinhardtii has been studied by vibrational spectroscopy. The FMN…”
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Spectroscopic Characterization of Flavin Mononucleotide Bound to the LOV1 Domain of Phot1 from Chlamydomonas reinhardtii by Holzer, W., Penzkofer, A., Fuhrmann, M., Hegemann, P.

“…The absorption and emission behavior of flavin mononucleotide (FMN) in the light-, oxygen- and voltage-sensitive (LOV) domain LOV1 of the photoreceptor Phot1…”
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Photophysical characterisation and photo-cycle dynamics of LOV1-His domain of phototropin from Chlamydomonas reinhardtii with roseoflavin monophosphate cofactor by Tyagi, A., Penzkofer, A., Mathes, T., Hegemann, P.

“…The wild-type phototropin protein phot from the green alga Chlamydomonas reinhardtii with the blue-light photoreceptor domains LOV1 and LOV2 has flavin…”
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Photodynamics of the small BLUF protein BlrB from Rhodobacter sphaeroides by Zirak, P., Penzkofer, A., Schiereis, T., Hegemann, P., Jung, A., Schlichting, I.

“…The BLUF protein BlrB from the non-sulphur anoxyphototrophic purple bacterium Rhodobacter sphaeroides is characterized by absorption and emission spectroscopy…”
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Absorption and fluorescence spectroscopic characterization of BLUF domain of AppA from Rhodobacter sphaeroides by Zirak, P., Penzkofer, A., Schiereis, T., Hegemann, P., Jung, A., Schlichting, I.

“…The BLUF domain of the transcriptional anti-repressor protein AppA from the non-sulfur anoxyphototrophic purple bacterium Rhodobacter sphaeroides was…”
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Absorption and emission spectroscopic characterization of blue-light receptor Slr1694 from Synechocystis sp. PCC6803 by Zirak, P., Penzkofer, A., Lehmpfuhl, C., Mathes, T., Hegemann, P.

“…The BLUF protein Slr1694 from the cyanobacterium Synechocystis sp. PCC6803 is characterized by absorption and emission spectroscopy. Slr1694 expressed from E…”
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Absorption and emission spectroscopic characterization of BLUF protein Slr1694 from Synechocystis sp. PCC6803 with roseoflavin cofactor by Zirak, P., Penzkofer, A., Mathes, T., Hegemann, P.

“…The wild-type BLUF protein Slr1694 from Synechocystis sp. PCC6803 (BLUF = blue-light sensor using FAD) has flavin adenosine dinucleotide (FAD) as natural…”
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Fluoresence quenching of riboflavin in aqueous solution by methionin and cystein by Drössler, P., Holzer, W., Penzkofer, A., Hegemann, P.

“…The fluorescence quantum distributions, fluorescence quantum yields, and fluorescence lifetimes of riboflavin in methanol, DMSO, water, and aqueous solutions…”
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Photopysical and photochemical excitation and relaxation dynamics of LOV domains of phot from Chlamydomonas reinhardtii by Holzer, W., Penzkofer, A., Hegemann, P.

“…The absorption and emission behaviour of flavin mononucleotide (FMN) in the wild-type light, oxygen and voltage-sensitive (LOV) domains LOV1 and LOV2 of the…”
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Photo-reduction of flavin mononucleotide to semiquinone form in LOV domain mutants of blue-light receptor phot from Chlamydomonas reinhardtii by Song, S.-H., Dick, B., Penzkofer, A., Hegemann, P.

“…The photo-excitation dynamics of the mutants LOV1-C57S and LOV2-C250S of the LOV-domains of the phototropin photoreceptor phot from the green alga…”
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Functional variations among LOV domains as revealed by FT-IR difference spectroscopy by Bednarz, T, Losi, A, Gartner, W, Hegemann, P, Heberle, J

“…The two LOV domains, LOV1 and LOV2, from Chlamydomonas reinhardtii were investigated by light-induced FT-IR difference spectroscopy and compared to the LOV…”
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