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  Characterization and X-ray structure of the NADH-dependent coenzyme A disulfide reductase from Thermus thermophilus

Lencina, A. M., Koepke, J., Preu, J., Münke, C., Gennis, R. B., Michel, H., et al. (2019). Characterization and X-ray structure of the NADH-dependent coenzyme A disulfide reductase from Thermus thermophilus. Biochimica et Biophysica Acta, Bioenergetics, 1860(11): e148080. doi:10.1016/j.bbabio.2019.148080.

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 Creators:
Lencina, Andrea M.1, Author
Koepke, Jürgen2, Author              
Preu, Julia2, Author              
Münke, Cornelia2, Author              
Gennis, Robert B.1, Author
Michel, Hartmut2, Author              
Schurig-Briccio, Lici A.1, Author
Affiliations:
1Department of Biochemistry, University of Illinois, 600 S. Mathews Street, Urbana, IL 61801, USA, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Coenzyme A disulfide reductase; NADH oxidation; X-ray structure; Flavoprotein; Thermus thermophilus
 Abstract: The crystal structure of the enzyme previously characterized as a type-2 NADH:menaquinone oxidoreductase (NDH-2) from Thermus thermophilus has been solved at a resolution of 2.9 Å and revealed that this protein is, in fact, a coenzyme A-disulfide reductase (CoADR). Coenzyme A (CoASH) replaces glutathione as the major low molecular weight thiol in Thermus thermophilus and is maintained in the reduced state by this enzyme (CoADR). Although the enzyme does exhibit NADH:menadione oxidoreductase activity expected for NDH-2 enzymes, the specific activity with CoAD as an electron acceptor is about 5-fold higher than with menadione. Furthermore, the crystal structure contains coenzyme A covalently linked Cys44, a catalytic intermediate (Cys44-S-S-CoA) reduced by NADH via the FAD cofactor. Soaking the crystals with menadione shows that menadione can bind to a site near the redox active FAD, consistent with the observed NADH:menadione oxidoreductase activity. CoADRs from other species were also examined and shown to have measurable NADH:menadione oxidoreductase activity. Although a common feature of this family of enzymes, no biological relevance is proposed. The CoADR from T. thermophilus is a soluble homodimeric enzyme. Expression of the recombinant TtCoADR at high levels in E. coli results in a small fraction that co-purifies with the membrane fraction, which was used previously to isolate the enzyme wrongly identified as a membrane-bound NDH-2. It is concluded that T. thermophilus does not contain an authentic NDH-2 component in its aerobic respiratory chain.

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Language(s): eng - English
 Dates: 2019-08-282019-05-312019-09-082019-09-112019-11-01
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbabio.2019.148080
 Degree: -

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Title: Biochimica et Biophysica Acta, Bioenergetics
  Abbreviation : Biochim. Biophys. Acta, Bioenerg.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1860 (11) Sequence Number: e148080 Start / End Page: - Identifier: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6