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Dark-Operative Protochlorophyllide Oxidoreductase

  1. Jürgen Moser1,
  2. Wolf-Dieter Schubert2

Published Online: 15 SEP 2012

DOI: 10.1002/9781119951438.eibc2059

Encyclopedia of Inorganic and Bioinorganic Chemistry

Encyclopedia of Inorganic and Bioinorganic Chemistry

How to Cite

Moser, J. and Schubert, W.-D. 2012. Dark-Operative Protochlorophyllide Oxidoreductase. Encyclopedia of Inorganic and Bioinorganic Chemistry. .

Author Information

  1. 1

    Institut für Mikrobiologie, Technische Universität Braunschweig, Braunschweig, Germany

  2. 2

    University of the Western Cape, Department of Biotechnology, Cape Town, South Africa

Publication History

  1. Published Online: 15 SEP 2012


Dark-operative (or light-independent) protochlorophyllide oxidoreductase is an enzyme of the chlorophyll and bacteriochlorophyll biosynthetic pathway catalyzing the reduction of protochlorophyllide to chlorophyllide. DPOR catalysis involves the ATP-dependent, two-electron reduction and trans-hydrogenation of the C17–C18 double bond of the conjugated D ring system of protochlorophyllide converting the pheoporphyrin backbone of protochlorophyllide to a chlorin macrocycle characteristic of all chlorophylls. The process is mediated by the dynamic interaction of two DPOR subcomplexes, each carrying redox active 4Fe–4S clusters. We discuss all available structural and biochemical data on this enzyme and compare it to nitrogenase and other related enzyme systems.

3D Structure


  • chlorophyll biosynthesis;
  • bacteriochlorophyll biosynthesis;
  • metalloenzyme;
  • tetrapyrrole;
  • chlorophyllide;
  • ATP-dependent electron transfer