EPR study of 1Asp-3Cys ligated 4Fe-4S iron-sulfur cluster in NB-protein (BchN-BchB) of a dark-operative protochlorophyllide reductase complex

Toru Kondo, Jiro Nomata, Yuichi Fujita, Shigeru Itoh

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

Dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like enzyme, contains two [4Fe-4S] clusters, one in the L-protein ((BchL) 2) and the other in the NB-protein ((BchN-BchB)2). The reduced NB-cluster in the NB-protein, which is ligated by 1Asp/3Cys residues, showed a broad S = 3/2 electron paramagnetic resonance signal that is rather rare in [4Fe-4S] clusters. A 4Cys-ligated NB-cluster in the mutated variant BchB-D36C protein, in which the Asp36 was replaced by a Cys, gave a rhombic normal S = 1/2 signal and lost the catalytic activity. The results suggest that Asp36 contributes to the low redox potential necessary to reduce protochlorophyllide.

Original languageEnglish
Pages (from-to)214-218
Number of pages5
JournalFEBS Letters
Volume585
Issue number1
DOIs
Publication statusPublished - 2011 Jan 3
Externally publishedYes

Keywords

  • Bacteriochlorophyll biosynthesis
  • BchB
  • BchN
  • Electron paramagnetic resonance
  • Iron-sulfur cluster
  • Protochlorophyllide

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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