Publications by the same author
plus in the repository
plus in Google Scholar

Bibliografische Daten exportieren
 

Reduction Midpoint Potential of a Paradigm Light-Oxygen-Voltage Receptor and its Modulation by Methionine Residues

DOI zum Zitieren der Version auf EPub Bayreuth: https://doi.org/10.15495/EPub_UBT_00008118
URN to cite this document: urn:nbn:de:bvb:703-epub-8118-8

Title data

García de Fuentes, Andrés ; Möglich, Andreas:
Reduction Midpoint Potential of a Paradigm Light-Oxygen-Voltage Receptor and its Modulation by Methionine Residues.
In: RSC Chemical Biology. Vol. 5 (2024) Issue 6 . - pp. 530-543.
ISSN 2633-0679
DOI der Verlagsversion: https://doi.org/10.1039/D4CB00056K

[thumbnail of d4cb00056k.pdf]
Format: PDF
Name: d4cb00056k.pdf
Version: Published Version
Available under License Creative Commons BY 3.0: Attribution
Download (2MB)

Project information

Project financing: Deutsche Forschungsgemeinschaft

Abstract

Light-dependent adaptations of organismal physiology, development, and behavior abound in nature and depend on sensory photoreceptors. As one class, light-oxygen-voltage (LOV) photoreceptors harness flavin-nucleotide chromophores to sense blue light. Photon absorption drives the LOV receptor to its signaling state, characterized by a metastable thioadduct between the flavin and a conserved cysteine residue. With this cysteine absent, LOV receptors instead undergo photoreduction to the flavin semiquinone which however can still elicit downstream physiological responses. Irrespective of the cysteine presence, the LOV photochemical response thus entails a formal reduction of the flavin. Against this backdrop, we here investigate the reduction midpoint potential E0 in the paradigm LOV2 domain from Avena sativa phototropin 1 (AsLOV2), and how it can be deliberately varied. Replacements of residues at different sites near the flavin by methionine consistently increase E0 from its value of around –280 mV by up to 40 mV. Moreover, methionine introduction invariably impairs photoactivation efficiency and thus renders the resultant AsLOV2 variants less light-sensitive. Although individual methionine substitutions also affect the stability of the signaling state and downstream allosteric responses, no clear-cut correlation with the redox properties emerges. With a reduction midpoint potential near –280 mV, AsLOV2 and, by inference, other LOV receptors may be partially reduced inside cells which directly affects their light responsiveness. The targeted modification of the chromophore environment, as presently demonstrated, may mitigate this effect and enables the design of LOV receptors with stratified redox sensitivities.

Further data

Item Type: Article in a journal
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry II - Photobiochemistry > Chair Biochemistry II - Photobiochemistry - Univ.-Prof. Dr. Andreas Möglich
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry I - Proteinbiochemie der Signaltransduktion
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry II - Photobiochemistry
Language: English
Originates at UBT: Yes
URN: urn:nbn:de:bvb:703-epub-8118-8
Date Deposited: 13 Jan 2025 07:47
Last Modified: 13 Jan 2025 07:47
URI: https://epub.uni-bayreuth.de/id/eprint/8118

Downloads

Downloads per month over past year