The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach

Jatindra N. Tripathy, Masakazu Hirasawa, Sung Kun Kim, Aaron T. Setterdahl, James P. Allen, David B. Knaff

Research output: Contribution to journalArticle

9 Citations (Scopus)


A system has been developed for expressing a His-tagged form of the ferredoxin-dependent nitrite reductase of spinach in Escherichia coli. The catalytic and spectral properties of the His-tagged, recombinant enzyme are similar, but not identical, to those previously observed for nitrite reductase isolated directly from spinach leaf. A detailed comparison of the spectral, catalytic and fluorescence properties of nitrite reductase variants, in which each of the enzyme's eight tryptophan residues has been replaced using site-directed mutagenesis by either aromatic or non-aromatic amino acids, has been used to examine possible roles for tryptophan residues in the reduction of nitrite to ammonia catalyzed by the enzyme.

Original languageEnglish
Pages (from-to)1-12
Number of pages12
JournalPhotosynthesis Research
Issue number1
Publication statusPublished - Oct 1 2007



  • Ferredoxin
  • Nitrite reductase
  • Tryptophan

ASJC Scopus subject areas

  • Biochemistry
  • Plant Science
  • Cell Biology

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