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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 385, Issue 10

Issues

Structural basis of denitrification

Oliver Einsle
  • Abt. Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Justus-von-Liebig-Weg 11, D-37077 Göttingen, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Peter M.H. Kroneck
  • Mathematisch-naturwissenschaftliche Sektion, Fachbereich Biologie, Universität Konstanz, Universitätsstrasse 10, D-78457 Konstanz, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2004.115

Abstract

Denitrification represents an important part of the biogeochemical cycle of the essential element nitrogen. It constitutes the predominant pathway of the reductive dissimilation of nitrate in the environment. Via four enzymatic reactions, nitrate is transformed stepwise to nitrite (NO2 -), nitric oxide (NO), and nitrous oxide (N2O), to finally yield dinitrogen gas (N2). All steps within this metabolic pathway are catalyzed by complex multi-site metalloenzymes with unique spectroscopic and structural features. In recent years, high-resolution crystal structures have become available for these enzymes with the exception of the structure for NO reductase.

Keywords: denitrification; nitrate reductase; nitrite reductase; nitric oxide reductase; nitrous oxide reductase

About the article

Published Online: 2005-06-01

Published in Print: 2004-10-01


Citation Information: Biological Chemistry, Volume 385, Issue 10, Pages 875–883, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2004.115.

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