FEBS Letters
Volume 580, Issue 26 , Pages 6151-6154, 13 November 2006

Nitrogenase Fe protein-like Fe–S cluster is conserved in L-protein (BchL) of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus

Edited by Richard Cogdell

  • Jiro Nomata

      Affiliations

    • Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
    • ,
  • Masaharu Kitashima

      Affiliations

    • Department of Biological Sciences, Kanagawa University, Hiratsuka, Kanagawa 259-1293, Japan
    • ,
  • Kazuhito Inoue

      Affiliations

    • Department of Biological Sciences, Kanagawa University, Hiratsuka, Kanagawa 259-1293, Japan
    • ,
  • Yuichi Fujita

      Affiliations

    • Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
    • Corresponding Author InformationCorresponding author. Fax: +81 52 789 4107.

Received 22 September 2006; received in revised form 7 October 2006; accepted 9 October 2006. published online 17 October 2006.

Abstract 

Dark-operative protochlorophyllide reductase (DPOR) in bacteriochlorophyll biosynthesis is a nitrogenase-like enzyme consisting of L-protein (BchL-dimer) as a reductase component and NB-protein (BchN–BchB-heterotetramer) as a catalytic component. Metallocenters of DPOR have not been identified. Here we report that L-protein has an oxygen-sensitive [4Fe–4S] cluster similar to nitrogenase Fe protein. Purified L-protein from Rhodobacter capsulatus showed absorption spectra and an electron paramagnetic resonance signal indicative of a [4Fe–4S] cluster. The activity quickly disappeared upon exposure to air with a half-life of 20s. These results suggest that the electron transfer mechanism is conserved in nitrogenase Fe protein and DPOR L-protein.

Abbreviations: Pchlide, protochlorophyllide, EPR, electron paramagnetic resonance, DPOR, dark-operative protochlorophyllide oxidoreductase, Chl, chlorophyll, BChl, bacteriochlorophyll, Chlide, chlorophyllide a

Keywords: Protochlorophyllide reductase, Nitrogenase, Bacteriochlorophyll biosynthesis, BchL, Fe–S cluster, Rhodobacter capsulatus

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PII: S0014-5793(06)01220-8

doi:10.1016/j.febslet.2006.10.014

FEBS Letters
Volume 580, Issue 26 , Pages 6151-6154, 13 November 2006

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