Lactococcus lactis Thioredoxin Reductase Is Sensitive to Light Inactivation-Reference-Cited by-同舟云学术

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Lactococcus lactis Thioredoxin Reductase Is Sensitive to Light Inactivation

Published:2015-02-20 Issue:8 Volume:54 Page:1628-1637
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Björnberg Olof¹,Viennet Thibault¹,Skjoldager Nicklas¹,Ćurović Aida¹,Nielsen Kristian Fog²,Svensson Birte¹,Hägglund Per¹

Affiliation:

1. Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Building 224, Søltofts Plads, DK-2800 Kongens Lyngby, Denmark

2. Metabolic Signaling and Regulation group, Department of Systems Biology, Technical University of Denmark, Building 221, Søltofts Plads, DK-2800 Kongens Lyngby, Denmark

Funder

Carlsbergfondet

Det Frie Forskningsråd | Teknologi og Produktion

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi5013639

Reference63 articles.

1. Physiological functions of thioredoxin and thioredoxin reductase

2. The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

3. Crystal Structure and Catalysis of the Selenoprotein Thioredoxin Reductase 1

4. Active sites of thioredoxin reductases: Why selenoproteins?

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