The Role of Tryptophan in the Ferredoxin-dependent Nitrite Reductase of Spinach

Overview

Journal Photosynth Res

Publisher Springer

Date 2007 Jul 6

PMID 17611813

Citations 4

Authors

Jatindra N Tripathy

Masakazu Hirasawa

Sung-Kun Kim

Aaron T Setterdahl

James P Allen

David B Knaff

Affiliations

Soon will be listed here.

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.

Citing Articles

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Enzymatic properties of the ferredoxin-dependent nitrite reductase from Chlamydomonas reinhardtii. Evidence for hydroxylamine as a late intermediate in ammonia production.

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The interaction of spinach nitrite reductase with ferredoxin: a site-directed mutation study.

Hirasawa M, Tripathy J, Somasundaram R, Johnson M, Bhalla M, Allen J Mol Plant. 2009; 2(3):407-15.

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Pattern of expression and substrate specificity of chloroplast ferredoxins from Chlamydomonas reinhardtii.

Terauchi A, Lu S, Zaffagnini M, Tappa S, Hirasawa M, Tripathy J J Biol Chem. 2009; 284(38):25867-78.

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