Publications by authors named "U Liebl"
Photoreduction of oxidized flavins has a functional role in photocatalytic and photoreceptor flavoproteins. In flavoproteins without light-dependent physiological functions, ultrafast, reversible flavin photoreduction is supposedly photoprotective by nature, and holds potential for nonnatural photocatalytic applications. In this work, we combine protein mutagenesis, ultrafast spectroscopy, molecular dynamics simulations and quantum mechanics calculations to investigate the nonfunctional flavin photoreduction in a flavoenzyme, lysine-specific demethylase 1 (LSD1) which is pivotal in DNA transcription.
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- - Asgard archaea are closely related to the ancestors of eukaryotes, and this study explores the evolution and function of thymidylate synthases and other enzymes crucial for DNA, RNA, and amino acid biosynthesis.
- - The research shows that Asgard enzymes have likely been acquired from bacteria through horizontal gene transfer and identifies that thymidylate synthase from a specific Asgard archaeon can utilize bacterial-like folates while responding to bacterial enzyme inhibitors.
- - The findings suggest that eukaryotic cells' ability to replicate DNA is influenced by both archaeal and bacterial traits, indicating that ongoing gene transfer from bacteria has significantly impacted Asgard archaea’s metabolic processes.
Carbon monoxide has been recognized relatively recently as signaling molecule, and only very few dedicated natural CO sensor proteins have been identified so far. These include in particular heme-based transcription factors: the bacterial sensor proteins CooA and RcoM. In these 6-coordinated systems, exchange between an internal protein residue and CO as a heme ligand in the sensor domain affects the properties of the DNA-binding domain.
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- Heme plays a key role in helping the bacterium Rhodobacter sphaeroides control when to make proteins for photosynthesis by interacting with two proteins called AppA and PpsR.
- Scientists used special techniques to study how heme binds to PpsR and affects its behavior, showing that this binding changes how the proteins work together.
- The research found that when heme attaches to PpsR, it helps the protein stick to DNA better, showing how heme is important for controlling gene activity in these bacteria.
Flavins are highly versatile redox-active and colored cofactors in a large variety of proteins. These do include photoenzymes and photoreceptors, although the vast majority performs non-light-driven physiological functions. Nevertheless, electron transfer between flavins and specific nearby amino acid residues (in particular tyrosine, tryptophan, and presumably histidine and arginine) takes place upon excitation of flavin in many flavoproteins.
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