NeoR, a near-infrared absorbing rhodopsin

Matthias Broser (), Anika Spreen, Patrick E. Konold, Enrico Schiewer, Suliman Adam, Veniamin Borin, Igor Schapiro, Reinhard Seifert, John T. M. Kennis, Yinth Andrea Bernal Sierra and Peter Hegemann
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Matthias Broser: Institute for Biology, Experimental Biophysics, Humboldt-Universität zu Berlin
Anika Spreen: Institute for Biology, Experimental Biophysics, Humboldt-Universität zu Berlin
Patrick E. Konold: Vrije Universiteit Amsterdam
Enrico Schiewer: Institute for Biology, Experimental Biophysics, Humboldt-Universität zu Berlin
Suliman Adam: Fritz Haber Center for Molecular Dynamics, Institute of Chemistry, The Hebrew University of Jerusalem
Veniamin Borin: Fritz Haber Center for Molecular Dynamics, Institute of Chemistry, The Hebrew University of Jerusalem
Igor Schapiro: Fritz Haber Center for Molecular Dynamics, Institute of Chemistry, The Hebrew University of Jerusalem
Reinhard Seifert: Molecular Sensory Systems, Center of Advanced European Studies and Research (caesar)
John T. M. Kennis: Vrije Universiteit Amsterdam
Yinth Andrea Bernal Sierra: Institute for Biology, Experimental Biophysics, Humboldt-Universität zu Berlin
Peter Hegemann: Institute for Biology, Experimental Biophysics, Humboldt-Universität zu Berlin

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract The Rhizoclosmatium globosum genome encodes three rhodopsin-guanylyl cyclases (RGCs), which are predicted to facilitate visual orientation of the fungal zoospores. Here, we show that RGC1 and RGC2 function as light-activated cyclases only upon heterodimerization with RGC3 (NeoR). RGC1/2 utilize conventional green or blue-light-sensitive rhodopsins (λmax = 550 and 480 nm, respectively), with short-lived signaling states, responsible for light-activation of the enzyme. The bistable NeoR is photoswitchable between a near-infrared-sensitive (NIR, λmax = 690 nm) highly fluorescent state (QF = 0.2) and a UV-sensitive non-fluorescent state, thereby modulating the activity by NIR pre-illumination. No other rhodopsin has been reported so far to be functional as a heterooligomer, or as having such a long wavelength absorption or high fluorescence yield. Site-specific mutagenesis and hybrid quantum mechanics/molecular mechanics simulations support the idea that the unusual photochemical properties result from the rigidity of the retinal chromophore and a unique counterion triad composed of two glutamic and one aspartic acids. These findings substantially expand our understanding of the natural potential and limitations of spectral tuning in rhodopsin photoreceptors.

Date: 2020
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DOI: 10.1038/s41467-020-19375-8

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