ArticleThe Journal of biological chemistry2013
Breaking the carboxyl rule: lysine 96 facilitates reprotonation of the Schiff base in the photocycle of a retinal protein from Exiguobacterium sibiricum.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 47 citations in OpenAlex.
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- Structural insights into light harvesting by antenna-containing rhodopsins in marine Asgard archaea.Nature microbiology · 2025Article
- Energetics of the H-Bond Network inBiochemistry · 2024Article
- Oriented Insertion of ESR-Containing Hybrid Proteins in Proteoliposomes.International journal of molecular sciences · 2023Article
- Application of direct electrometry in studies of microbial rhodopsins reconstituted in proteoliposomes.Biophysical reviews · 2022Review
- Structural characterization of proton-pumping rhodopsin lacking a cytoplasmic proton donor residue by X-ray crystallography.The Journal of biological chemistry · 2022Article
- Diversity, Mechanism, and Optogenetic Application of Light-Driven Ion Pump Rhodopsins.Advances in experimental medicine and biology · 2021Review
- Mechanism of formate-nitrite transporters by dielectric shift of substrate acidity.The EMBO journal · 2017Article
- Insights into the structure and function of HV1 from a meta-analysis of mutation studies.The Journal of general physiology · 2016Review
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- A new class of marine Euryarchaeota group II from the Mediterranean deep chlorophyll maximum.The ISME journal · 2015Article
- Ion-pumping microbial rhodopsins.Frontiers in molecular biosciences · 2015Review
- Light-driven Na(+) pump from Gillisia limnaea: a high-affinity Na(+) binding site is formed transiently in the photocycle.Biochemistry · 2014Article
- Nature's toolkit for microbial rhodopsin ion pumps.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Photocycle of Exiguobacterium sibiricum rhodopsin characterized by low-temperature trapping in the IR and time-resolved studies in the visible.The journal of physical chemistry. B · 2013Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
A lysine instead of the usual carboxyl group is in place of the internal proton donor to the retinal Schiff base in the light-driven proton pump of Exiguobacterium sibiricum (ESR). The involvement of this lysine in proton transfer is indicated by the finding that its substitution with alanine or other residues slows reprotonation of the Schiff base (decay of the M intermediate) by more than 2 orders of magnitude. In these mutants, the rate constant of the M decay linearly decreases with a decrease in proton concentration, as expected if reprotonation is limited by the uptake of a proton from the bulk. In wild type ESR, M decay is biphasic, and the rate constants are nearly pH-independent between pH 6 and 9. Proton uptake occurs after M formation but before M decay, which is especially evident in D2O and at high pH. Proton uptake is biphasic; the amplitude of the fast phase decreases with a pKa of 8.5 ± 0.3, which reflects the pKa of the donor during proton uptake. Similarly, the fraction of the faster component of M decay decreases and the slower one increases, with a pKa of 8.1 ± 0.2. The data therefore suggest that the reprotonation of the Schiff base in ESR is preceded by transient protonation of an initially unprotonated donor, which is probably the ε-amino group of Lys-96 or a water molecule in its vicinity, and it facilitates proton delivery from the bulk to the reaction center of the protein.
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