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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 394, Issue 5 (May 2013)

Issues

Alternate pathways for NADH oxidation in Thermus thermophilus using type 2 NADH dehydrogenases

Padmaja Venkatakrishnan
  • Department of Biochemistry, University of Illinois, 600 S. Mathews Street, Urbana, IL 61801, USA
  • Other articles by this author:
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/ Andrea M. Lencina
  • Department of Biochemistry, University of Illinois, 600 S. Mathews Street, Urbana, IL 61801, USA
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/ Lici A. Schurig-Briccio
  • Corresponding author
  • Department of Biochemistry, University of Illinois, 600 S. Mathews Street, Urbana, IL 61801, USA
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/ Robert B. Gennis
  • Corresponding author
  • Department of Biochemistry, University of Illinois, 600 S. Mathews Street, Urbana, IL 61801, USA
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Published Online: 2013-01-31 | DOI: https://doi.org/10.1515/hsz-2012-0333

Abstract

Type 2 NADH dehydrogenase (NDH-2) is a single-subunit membrane-associated flavoenzyme that is part of the respiratory chain of many prokaryotes. The enzyme catalyzes the electron transfer from NADH to quinone but is not directly coupled to the generation of a proton motive force. The purpose of the current work is to compare two different NDH-2s that are encoded in strains of Thermus thermophilus. The aerobic T. thermophilus HB27 strain expresses one NDH-2 that has been previously isolated and characterized. In this work it is shown that a gene, which is misannotated as an NADH oxidase, encodes this enzyme. Unlike HB27, strain NAR1 of T. thermophilus is capable of partial denitrification, and in addition its genome contains the nrcN gene that encodes a second putative NDH-2. Of particular interest is the fact that nrcN is part of an operon (nrcDEFN) that is proposed to encode a protein complex specifically required for nitrate reduction. In this work, the nrcN gene has the activity expected of a NDH-2, and functions independently of other components of the putative Nrc complex. The biochemical properties of the two NDH-2 enzymes are compared. Efforts to demonstrate that NrcN is part of a multiprotein complex were not successful. However, the NrcE protein was expressed in Escherichia coli and shown to be a membrane-bound protein containing heme B.

Keywords: flavoprotein; membrane bound protein; nitrate reduction; Nrc complex; thermophilic enzymes

About the article

Corresponding authors: Lici A. Schurig-Briccio and Robert B. Gennis, Department of Biochemistry, University of Illinois, 600 S. Mathews Street, Urbana, IL 61801, USA


Received: 2012-11-21

Accepted: 2013-01-24

Published Online: 2013-01-31

Published in Print: 2013-05-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2012-0333.

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©2013 by Walter de Gruyter Berlin Boston. Copyright Clearance Center

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[2]
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