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. 2007 Oct;94(1):1-12.
doi: 10.1007/s11120-007-9198-5. Epub 2007 Jul 5.

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

Jatindra N Tripathy  1 , Masakazu Hirasawa, Sung-Kun Kim, Aaron T Setterdahl, James P Allen, David B Knaff
Affiliations

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

Jatindra N Tripathy et al. Photosynth Res. 2007 Oct.

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.

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