ArticleScientific reports2017
The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 12 citations in OpenAlex.
- Photo-Oxidation of Therapeutic Protein Formulations: From Radical Formation to Analytical Techniques.Pharmaceutics · 2021Review
- Thioredoxin reductase from Bacillus cereus exhibits distinct reduction and NADPH-binding properties.FEBS open bio · 2021Article
- Stabilisation of the Fatty Acid Decarboxylase from Chlorella variabilis by Caprylic Acid.Chembiochem : a European journal of chemical biology · 2021Article
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Authors and funding
8 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The NADPH-dependent homodimeric flavoenzyme thioredoxin reductase (TrxR) provides reducing equivalents to thioredoxin, a key regulator of various cellular redox processes. Crystal structures of photo-inactivated thioredoxin reductase (TrxR) from the Gram-positive bacterium Lactococcus lactis have been determined. These structures reveal novel molecular features that provide further insight into the mechanisms behind the sensitivity of this enzyme toward visible light. We propose that a pocket on the si-face of the isoalloxazine ring accommodates oxygen that reacts with photo-excited FAD generating superoxide and a flavin radical that oxidize the isoalloxazine ring C7α methyl group and a nearby tyrosine residue. This tyrosine and key residues surrounding the oxygen pocket are conserved in enzymes from related bacteria, including pathogens such as Staphylococcus aureus. Photo-sensitivity may thus be a widespread feature among bacterial TrxR with the described characteristics, which affords applications in clinical photo-therapy of drug-resistant bacteria.
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