Abstract
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 language | English (US) |
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Pages (from-to) | 1-12 |
Number of pages | 12 |
Journal | Photosynthesis research |
Volume | 94 |
Issue number | 1 |
DOIs | |
State | Published - Oct 2007 |
Keywords
- Ferredoxin
- Nitrite reductase
- Tryptophan
ASJC Scopus subject areas
- Biochemistry
- Plant Science
- Cell Biology