Absorption and Emission Spectroscopic Investigation of Thermal Dynamics and Photo-Dynamics of the Rhodopsin Domain of the Rhodopsin-Guanylyl Cyclase from the Nematophagous Fungus Catenaria anguillulae

URN to cite this document:

urn:nbn:de:bvb:355-epub-365415 Copy

DOI to cite this document:

10.5283/epub.36541 Copy

Penzkofer, Alfons ; Scheib, Ulrike ; Stehfest, Katja ; Hegemann, Peter

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License: Creative Commons Attribution 4.0 PDF - Published Version (7MB)

Date of publication of this fulltext: 19 Jan 2018 15:47

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Details

Item type:	Article
Open Access Type:	Gold (with APC)
Höhe Gebühr (aus OpenAPC):	1671.26
Institution der Zahlung:	Regensburg U
Journal or Publication Title:	International Journal of Molecular Sciences
Publisher:	MDPI
Place of Publication:	BASEL
Volume:	18
Number of Issue or Book Chapter:	10
Page Range:	p. 2099
Date:	5 October 2017
Institutions:	Physics > Institute of Experimental and Applied Physics > Alumni or Retired Professors > Group Alfons Penzkofer
Projects (Historical):	Open Access Publizieren (DFG)
Identification Number:	Value Type 10.3390/ijms18102099 DOI
Keywords:	LIGHT-DARK ADAPTATION; SCHIFF-BASE; FLUORESCENCE; PROTEIN; CHANNELRHODOPSIN; BACTERIORHODOPSIN; DEPROTONATION; MOLECULES; LIFETIME; BEHAVIOR; rhodopsin domain; rhodopsin-guanylyl cyclase; nematophagous fungus Catenaria anguillulae; retinal Schiff base; primary photocycle dynamics; secondary photocycle dynamics; photo-degradation
Dewey Decimal Classification:	500 Science > 530 Physics
Status:	Published
Refereed:	Yes, this version has been refereed
Created at the University of Regensburg:	Yes
Item ID:	36541

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Abstract

The rhodopsin-guanylyl cyclase from the nematophagous fungus Catenaria anguillulae belongs to a recently discovered class of enzymerhodopsins and may find application as a tool in optogenetics. Here the rhodopsin domain CaRh of the rhodopsin-guanylyl cyclase from Catenaria anguillulae was studied by absorption and emission spectroscopic methods. The absorption cross-section spectrum and ...

Abstract

The rhodopsin-guanylyl cyclase from the nematophagous fungus Catenaria anguillulae belongs to a recently discovered class of enzymerhodopsins and may find application as a tool in optogenetics. Here the rhodopsin domain CaRh of the rhodopsin-guanylyl cyclase from Catenaria anguillulae was studied by absorption and emission spectroscopic methods. The absorption cross-section spectrum and excitation wavelength dependent fluorescence quantum distributions of CaRh samples were determined (first absorption band in the green spectral region). The thermal stability of CaRh was studied by long-time attenuation measurements at room temperature (20.5 degrees C) and refrigerator temperature of 3.5 degrees C. The apparent melting temperature of CaRh was determined by stepwise sample heating up and cooling down (obtained apparent melting temperature: 62 +/- 2 degrees C). The photocycle dynamics of CaRh was investigated by sample excitation to the first inhomogeneous absorption band of the CaRhda dark-adapted state around 590 nm (long-wavelength tail), 530 nm (central region) and 470 nm (short-wavelength tail) and following the absorption spectra development during exposure and after exposure (time resolution 0.0125 s). The original protonated retinal Schiff base PRSBall-trans in CaRhda photo-converted reversibly to protonated retinal Schiff base PRSBall-trans, la1 with restructured surroundings (CaRhla1 light-adapted state, slightly blue-shifted and broadened first absorption band, recovery to CaRhda with time constant of 0.8 s) and deprotonated retinal Schiff base RSB13-cis (CaRhla2 light-adapted state, first absorption band in violet to near ultraviolet spectral region, recovery to CaRhda with time constant of 0.35 s). Long-time light exposure of light-adapted CaRhla1 around 590, 530 and 470 nm caused low-efficient irreversible degradation to photoproducts CaRhprod. Schemes of the primary photocycle dynamics of CaRhda and the secondary photocycle dynamics of CaRhla1 are developed.

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