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  1. Article: Impact of protein-chromophore interaction on the retinal excited state and photocycle of

    Misra, Ramprasad / Das, Ishita / Dér, András / Steinbach, Gábor / Shim, Jin-Gon / Busse, Wayne / Jung, Kwang-Hwan / Zimányi, László / Sheves, Mordechai

    Chemical science

    2023  Volume 14, Issue 36, Page(s) 9951–9958

    Abstract: The function of microbial as well as mammalian retinal proteins ( ...

    Abstract The function of microbial as well as mammalian retinal proteins (
    Language English
    Publishing date 2023-09-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 2559110-1
    ISSN 2041-6539 ; 2041-6520
    ISSN (online) 2041-6539
    ISSN 2041-6520
    DOI 10.1039/d3sc02961a
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: The Functionality of the DC Pair in a Rhodopsin Guanylyl Cyclase from Catenaria anguillulae.

    Fischer, Paul / Schiewer, Enrico / Broser, Matthias / Busse, Wayne / Spreen, Anika / Grosse, Max / Hegemann, Peter / Bartl, Franz

    Journal of molecular biology

    2023  Volume 436, Issue 5, Page(s) 168375

    Abstract: Rhodopsin guanylyl cyclases (RGCs) belong to the class of enzymerhodopsins catalyzing the transition from GTP into the second messenger cGMP, whereas light-regulation of enzyme activity is mediated by a membrane-bound microbial rhodopsin domain, that ... ...

    Abstract Rhodopsin guanylyl cyclases (RGCs) belong to the class of enzymerhodopsins catalyzing the transition from GTP into the second messenger cGMP, whereas light-regulation of enzyme activity is mediated by a membrane-bound microbial rhodopsin domain, that holds the catalytic center inactive in the dark. Structural determinants for activation of the rhodopsin moiety eventually leading to catalytic activity are largely unknown. Here, we investigate the mechanistic role of the D283-C259 (DC) pair that is hydrogen bonded via a water molecule as a crucial functional motif in the homodimeric C. anguillulae RGC. Based on a structural model of the DC pair in the retinal binding pocket obtained by MD simulation, we analyzed formation and kinetics of early and late photocycle intermediates of the rhodopsin domain wild type and specific DC pair mutants by combined UV-Vis and FTIR spectroscopy at ambient and cryo-temperatures. By assigning specific infrared bands to S-H vibrations of C259 we are able to show that the DC pair residues are tightly coupled. We show that deprotonation of D283 occurs already in the inactive L state as a prerequisite for M state formation, whereas structural changes of C259 occur in the active M state and early cryo-trapped intermediates. We propose a comprehensive molecular model for formation of the M state that activates the catalytic moiety. It involves light induced changes in bond strength and hydrogen bonding of the DC pair residues from the early J state to the active M state and explains the retarding effect of C259 mutants.
    MeSH term(s) Blastocladiomycota/enzymology ; Blastocladiomycota/metabolism ; Guanylate Cyclase/chemistry ; Guanylate Cyclase/genetics ; Light ; Models, Molecular ; Rhodopsin/chemistry ; Rhodopsin/genetics ; Spectroscopy, Fourier Transform Infrared
    Chemical Substances Guanylate Cyclase (EC 4.6.1.2) ; Rhodopsin (9009-81-8)
    Language English
    Publishing date 2023-12-12
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2023.168375
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 867: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Diversity of rhodopsin cyclases in zoospore-forming fungi.

    Broser, Matthias / Busse, Wayne / Spreen, Anika / Reh, Maila / Bernal Sierra, Yinth Andrea / Hwang, Songhwan / Utesch, Tillmann / Sun, Han / Hegemann, Peter

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 44, Page(s) e2310600120

    Abstract: Light perception for orientation in zoospore-forming fungi is linked to homo- or heterodimeric rhodopsin-guanylyl cyclases (RGCs). Heterodimeric RGCs, first identified in the ... ...

    Abstract Light perception for orientation in zoospore-forming fungi is linked to homo- or heterodimeric rhodopsin-guanylyl cyclases (RGCs). Heterodimeric RGCs, first identified in the chytrid
    MeSH term(s) Animals ; Rhodopsin/genetics ; Retina ; Photoreceptor Cells ; Light ; Guanylate Cyclase/genetics ; Mammals
    Chemical Substances Rhodopsin (9009-81-8) ; Guanylate Cyclase (EC 4.6.1.2)
    Language English
    Publishing date 2023-10-23
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2310600120
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Multiple retinal isomerizations during the early phase of the bestrhodopsin photoreaction.

    Kaziannis, Spyridon / Broser, Matthias / van Stokkum, Ivo H M / Dostal, Jakub / Busse, Wayne / Munhoven, Arno / Bernardo, Cesar / Kloz, Miroslav / Hegemann, Peter / Kennis, John T M

    Proceedings of the National Academy of Sciences of the United States of America

    2024  Volume 121, Issue 12, Page(s) e2318996121

    Abstract: Bestrhodopsins constitute a class of light-regulated pentameric ion channels that consist of one or two rhodopsins in tandem fused with bestrophin ion channel domains. Here, we report on the isomerization dynamics in the rhodopsin tandem domains ... ...

    Abstract Bestrhodopsins constitute a class of light-regulated pentameric ion channels that consist of one or two rhodopsins in tandem fused with bestrophin ion channel domains. Here, we report on the isomerization dynamics in the rhodopsin tandem domains of
    MeSH term(s) Isomerism ; Protein Conformation ; Rhodopsin/metabolism ; Retinaldehyde/chemistry ; Diterpenes
    Chemical Substances Rhodopsin (9009-81-8) ; 13-cis-retinal (472-86-6) ; Retinaldehyde (RR725D715M) ; Diterpenes
    Language English
    Publishing date 2024-03-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2318996121
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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