The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage. / Skjoldager, Nicklas; Blanner Bang, Maria; Rykaer, Martin; Björnberg, Olof; Davies, Michael Jonathan; Svensson, Birte; Harris, Pernille; Hägglund, Per.

I: Scientific Reports, Bind 7, 46282, 04.2017.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Skjoldager, N, Blanner Bang, M, Rykaer, M, Björnberg, O, Davies, MJ, Svensson, B, Harris, P & Hägglund, P 2017, 'The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage', Scientific Reports, bind 7, 46282. https://doi.org/10.1038/srep46282

APA

Skjoldager, N., Blanner Bang, M., Rykaer, M., Björnberg, O., Davies, M. J., Svensson, B., Harris, P., & Hägglund, P. (2017). The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage. Scientific Reports, 7, [46282]. https://doi.org/10.1038/srep46282

Vancouver

Skjoldager N, Blanner Bang M, Rykaer M, Björnberg O, Davies MJ, Svensson B o.a. The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage. Scientific Reports. 2017 apr.;7. 46282. https://doi.org/10.1038/srep46282

Author

Skjoldager, Nicklas ; Blanner Bang, Maria ; Rykaer, Martin ; Björnberg, Olof ; Davies, Michael Jonathan ; Svensson, Birte ; Harris, Pernille ; Hägglund, Per. / The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage. I: Scientific Reports. 2017 ; Bind 7.

Bibtex

@article{b16fb1d1d13843cebb9f2a921333f75d,
title = "The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage",
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.",
keywords = "Journal Article",
author = "Nicklas Skjoldager and {Blanner Bang}, Maria and Martin Rykaer and Olof Bj{\"o}rnberg and Davies, {Michael Jonathan} and Birte Svensson and Pernille Harris and Per H{\"a}gglund",
year = "2017",
month = apr,
doi = "10.1038/srep46282",
language = "English",
volume = "7",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage

AU - Skjoldager, Nicklas

AU - Blanner Bang, Maria

AU - Rykaer, Martin

AU - Björnberg, Olof

AU - Davies, Michael Jonathan

AU - Svensson, Birte

AU - Harris, Pernille

AU - Hägglund, Per

PY - 2017/4

Y1 - 2017/4

N2 - 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.

AB - 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.

KW - Journal Article

U2 - 10.1038/srep46282

DO - 10.1038/srep46282

M3 - Journal article

C2 - 28397795

VL - 7

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 46282

ER -

ID: 182331076