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

Masakazu Hirasawa; Jatindra N. Tripathy; Ramasamy Somasundaram; Michael K. Johnson; Megha Bhalla; James Allen; David B. Knaff

doi:10.1093/mp/ssn098

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

Masakazu Hirasawa, Jatindra N. Tripathy, Ramasamy Somasundaram, Michael K. Johnson, Megha Bhalla, James Allen, David B. Knaff

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19 Scopus citations

Abstract

A series of site-directed mutants of the ferredoxin-dependent spinach nitrite reductase has been characterized and several amino acids have been identified that appear to be involved in the interaction of the enzyme with ferredoxin. In a complementary study, binding constants to nitrite reductase and steady-state kinetic parameters of site-directed mutants of ferredoxin were determined in an attempt to identify ferredoxin amino acids involved in the interaction with nitrite reductase. The results have been interpreted in terms of an in-silico docking model for the 1:1 complex of ferredoxin with nitrite reductase.

Original language	English (US)
Pages (from-to)	407-415
Number of pages	9
Journal	Molecular Plant
Volume	2
Issue number	3
DOIs	https://doi.org/10.1093/mp/ssn098
State	Published - May 2009

Keywords

Electron transport
Enzymology
Molecular biology
Nitrogen metabolism

ASJC Scopus subject areas

Molecular Biology
Plant Science

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10.1093/mp/ssn098

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title = "The interaction of spinach nitrite reductase with ferredoxin: A site-directed mutation study",

abstract = "A series of site-directed mutants of the ferredoxin-dependent spinach nitrite reductase has been characterized and several amino acids have been identified that appear to be involved in the interaction of the enzyme with ferredoxin. In a complementary study, binding constants to nitrite reductase and steady-state kinetic parameters of site-directed mutants of ferredoxin were determined in an attempt to identify ferredoxin amino acids involved in the interaction with nitrite reductase. The results have been interpreted in terms of an in-silico docking model for the 1:1 complex of ferredoxin with nitrite reductase.",

keywords = "Electron transport, Enzymology, Molecular biology, Nitrogen metabolism",

author = "Masakazu Hirasawa and Tripathy, {Jatindra N.} and Ramasamy Somasundaram and Johnson, {Michael K.} and Megha Bhalla and James Allen and Knaff, {David B.}",

note = "Funding Information: This work was supported by a contract from the Chemical Sciences, Geosciences and Biosciences Division, Office of the Basic Energy Sciences, Office of Sciences, U.S. Department of Energy (Contract No. DE-FG03-99ER20346 to DBK) and from a grant the U.S. National Institutes of Health ( GM62524 to MKJ), which provided funds for the EPR portions of the study. ",

year = "2009",

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doi = "10.1093/mp/ssn098",

language = "English (US)",

volume = "2",

pages = "407--415",

journal = "Molecular Plant",

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AU - Hirasawa, Masakazu

AU - Tripathy, Jatindra N.

AU - Somasundaram, Ramasamy

AU - Johnson, Michael K.

AU - Bhalla, Megha

AU - Allen, James

AU - Knaff, David B.

N1 - Funding Information: This work was supported by a contract from the Chemical Sciences, Geosciences and Biosciences Division, Office of the Basic Energy Sciences, Office of Sciences, U.S. Department of Energy (Contract No. DE-FG03-99ER20346 to DBK) and from a grant the U.S. National Institutes of Health ( GM62524 to MKJ), which provided funds for the EPR portions of the study.

PY - 2009/5

Y1 - 2009/5

N2 - A series of site-directed mutants of the ferredoxin-dependent spinach nitrite reductase has been characterized and several amino acids have been identified that appear to be involved in the interaction of the enzyme with ferredoxin. In a complementary study, binding constants to nitrite reductase and steady-state kinetic parameters of site-directed mutants of ferredoxin were determined in an attempt to identify ferredoxin amino acids involved in the interaction with nitrite reductase. The results have been interpreted in terms of an in-silico docking model for the 1:1 complex of ferredoxin with nitrite reductase.

AB - A series of site-directed mutants of the ferredoxin-dependent spinach nitrite reductase has been characterized and several amino acids have been identified that appear to be involved in the interaction of the enzyme with ferredoxin. In a complementary study, binding constants to nitrite reductase and steady-state kinetic parameters of site-directed mutants of ferredoxin were determined in an attempt to identify ferredoxin amino acids involved in the interaction with nitrite reductase. The results have been interpreted in terms of an in-silico docking model for the 1:1 complex of ferredoxin with nitrite reductase.

KW - Electron transport

KW - Enzymology

KW - Molecular biology

KW - Nitrogen metabolism

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EP - 415

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JF - Molecular Plant

IS - 3

ER -

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

Abstract

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