Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation.

Marti, T; Otto, H. H.; Mogi, Tatsushi; Rösselet, S J; Heyn, Maarten P.; Khorana, H G

doi:10.1016/s0021-9258(20)89590-8

Cited by 113 publications

(44 citation statements)

References 47 publications

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“…Furthermore, blue-absorbing RGC2 (λ MAX 480 nm) and greenabsorbing RGC1 (λ MAX 550 nm) from R. globosum also differ in this position. Other conserved residues close to the β-ionone ring, e.g., NeoR S191 (Figures 4A,D), again show similar blue-shifting [∼320 cm −1 NeoR (S191A)] capacity as observed in other microbial rhodopsins [∼240 cm −1 Gloeobacter Rhodopsin (S141A); ∼560 cm −1 BR (S141A) (Marti et al, 1991;Engqvist et al, 2015)]. Accordingly, the chromophore cavity of NeoR resembles a commonly observed impact for color-tuning and thus is not the structural feature that drives NIR-absorption of the protein.…”

Section: Nir-absorbing Neorhodopsinsupporting

confidence: 58%

“…Therefore, other interactions likely involving water-molecules and ions may account for stabilization of the RSBH + . Intensive experiments mutating the retinal binding pocket of microbial rhodopsins, particular of BR, have been undertaken to prove this concept (Derguini et al, 1983;Ahl et al, 1988;Mogi et al, 1988;Mogi et al, 1989;Marti et al, 1991;Greenhalgh et al, 1992;Greenhalgh et al, 1993). However, the results were not always conclusive, which may reflect the problem that introduced pointmutations potentially alter the integrity of the retinal binding pocket more globally than intended.…”

Section: Tuning the Spectral Properties Of Retinal Chromophoresmentioning

confidence: 99%

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Far-Red Absorbing Rhodopsins, Insights From Heterodimeric Rhodopsin-Cyclases

Broser

2022

Front. Mol. Biosci.

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The recently discovered Rhodopsin-cyclases from Chytridiomycota fungi show completely unexpected properties for microbial rhodopsins. These photoreceptors function exclusively as heterodimers, with the two subunits that have very different retinal chromophores. Among them is the bimodal photoswitchable Neorhodopsin (NeoR), which exhibits a near-infrared absorbing, highly fluorescent state. These are features that have never been described for any retinal photoreceptor. Here these properties are discussed in the context of color-tuning approaches of retinal chromophores, which have been extensively studied since the discovery of the first microbial rhodopsin, bacteriorhodopsin, in 1971 (Oesterhelt et al., Nature New Biology, 1971, 233 (39), 149–152). Further a brief review about the concept of heterodimerization is given, which is widely present in class III cyclases but is unknown for rhodopsins. NIR-sensitive retinal chromophores have greatly expanded our understanding of the spectral range of natural retinal photoreceptors and provide a novel perspective for the development of optogenetic tools.

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Section: Nir-absorbing Neorhodopsinsupporting

confidence: 58%

Section: Tuning the Spectral Properties Of Retinal Chromophoresmentioning

confidence: 99%

Far-Red Absorbing Rhodopsins, Insights From Heterodimeric Rhodopsin-Cyclases

Broser

2022

Front. Mol. Biosci.

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“…The role played by several of the proposed channel residues has been confirmed by mutagenesis experiments. [31][32][33][34][35][36] FTIR and fluorescence label- ing experiments have shown that the immediate environment around a number of key residues in the putative proton transfer pathway change during the photocycle. 37 It has been postulated that a select number of water molecules in the pathway play an important role in proton transport.…”

Section: Bacteriorhodopsin: Cavities and Proton Pathwaymentioning

confidence: 99%

Analytical shape computation of macromolecules: II. Inaccessible cavities in proteins

et al. 1998

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The structures of proteins are well-packed, yet they contain numerous cavities which play key roles in accommodating small molecules, or enabling conformational changes. From high-resolution structures it is possible to identify these cavities. We have developed a precise algorithm based on alpha shapes for measuring space-filling-based molecular models (such as van der Waals, solvent accessible, and molecular surface descriptions). We applied this method for accurate computation of the surface area and volume of cavities in several proteins. In addition, all of the atoms/residues lining the cavities are identified. We use this method to study the structure and the stability of proteins, as well as to locate cavities that could contain structural water molecules in the proton transport pathway in the membrane protein bacteriorhodopsin.

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“…The structure of a double mutant T90A/D115A (3cod) showed little difference from the wildtype (Joh et al, 2008) while the single mutants T90V and T90A retain < 70% and < 20% of the proton pumping activity, respectively (Marti et al, 1991; Perálvarez et al, 2001). These observations illustrate that some nonproductive pathways of the isomerization sampling succeed more in the altered retinal binding pocket.…”

Section: Resultsmentioning

confidence: 99%

Photoinduced Isomerization Sampling of Retinal in Bacteriorhodopsin

Ren

2021

Preprint

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Photoisomerization of retinoids inside a confined protein pocket represents a critical chemical event in many important biological processes from animal vision, non-visual light effects, to bacterial light sensing and harvesting. Light driven proton pumping in bacteriorhodopsin entails exquisite electronic and conformational reconfigurations during its photocycle. However, it has been a major challenge to delineate transient molecular events preceding and following the photoisomerization of the retinal from noisy electron density maps when varying populations of intermediates coexist and evolve as a function of time. Here I report several distinct early photoproducts deconvoluted from the recently observed mixtures in time-resolved serial crystallography. This deconvolution substantially improves the quality of the electron density maps hence demonstrates that the all-trans retinal undergoes extensive isomerization sampling before it proceeds to the productive 13-cis configuration. Upon light absorption, the chromophore attempts to perform trans-to-cis isomerization at every double bond coupled with the stalled anti-to-syn rotations at multiple single bonds along its polyene chain. Such isomerization sampling pushes all seven transmembrane helices to bend outward, resulting in a transient expansion of the retinal binding pocket, and later, a contraction due to recoiling. These ultrafast responses observed at the atomic resolution support that the productive photoreaction in bacteriorhodopsin is initiated by light-induced charge separation in the prosthetic chromophore yet governed by stereoselectivity of its protein pocket. The method of a numerical resolution of concurrent events from mixed observations is also generally applicable.

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Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation.

Cited by 113 publications

References 47 publications

Far-Red Absorbing Rhodopsins, Insights From Heterodimeric Rhodopsin-Cyclases

Far-Red Absorbing Rhodopsins, Insights From Heterodimeric Rhodopsin-Cyclases

Analytical shape computation of macromolecules: II. Inaccessible cavities in proteins

Photoinduced Isomerization Sampling of Retinal in Bacteriorhodopsin

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