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

doi:10.1007/s11120-007-9198-5

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

Center for BioTechnology Genomics

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

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
Pages (from-to)	1-12
Number of pages	12
Journal	Photosynthesis Research
Volume	94
Issue number	1
DOIs	https://doi.org/10.1007/s11120-007-9198-5
State	Published - Oct 2007

Keywords

Ferredoxin
Nitrite reductase
Tryptophan

Access to Document

10.1007/s11120-007-9198-5

Link to publication in Scopus

Fingerprint Dive into the research topics of 'The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach'. Together they form a unique fingerprint.

Cite this

@article{759c8c8a989e486f9be7d13092bd70c2,

title = "The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach",

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.",

keywords = "Ferredoxin, Nitrite reductase, Tryptophan",

author = "Tripathy, {Jatindra N.} and Masakazu Hirasawa and Kim, {Sung Kun} and Setterdahl, {Aaron T.} and Allen, {James P.} and Knaff, {David B.}",

year = "2007",

month = oct,

doi = "10.1007/s11120-007-9198-5",

language = "English",

volume = "94",

pages = "1--12",

journal = "Photosynthesis Research",

issn = "0166-8595",

number = "1",

}

TY - JOUR

T1 - The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach

AU - Tripathy, Jatindra N.

AU - Hirasawa, Masakazu

AU - Kim, Sung Kun

AU - Setterdahl, Aaron T.

AU - Allen, James P.

AU - Knaff, David B.

PY - 2007/10

Y1 - 2007/10

N2 - 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.

AB - 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.

KW - Ferredoxin

KW - Nitrite reductase

KW - Tryptophan

UR - http://www.scopus.com/inward/record.url?scp=34548154052&partnerID=8YFLogxK

U2 - 10.1007/s11120-007-9198-5

DO - 10.1007/s11120-007-9198-5

M3 - Article

C2 - 17611813

AN - SCOPUS:34548154052

VL - 94

SP - 1

EP - 12

JO - Photosynthesis Research

JF - Photosynthesis Research

SN - 0166-8595

IS - 1

ER -