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Molecular Plant 2009 2(3):407-415; doi:10.1093/mp/ssn098
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© The Author 2009. Published by the Molecular Plant Shanghai Editorial Office in association with Oxford University Press on behalf of CSPP and IPPE, SIBS, CAS.

The Interaction of Spinach Nitrite Reductase with Ferredoxin: A Site-Directed Mutation Study

Masakazu Hirasawaa, Jatindra N. Tripathya, Ramasamy Somasundaramb, Michael K. Johnsonb, Megha Bhallaa, James P. Allenc and David B. Knaffa,d,1

a Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409-1061, USA
b Department of Chemistry, University of Georgia, Athens, GA 30602, USA
c Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA
d Institute for Biotechnology and Genomics, Texas Tech University, Lubbock, TX 79409-1061, USA

1 To whom correspondence should be addressed. E-mail david.knaff{at}ttu.edu.

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.

Key Words: Electron transport • enzymology • nitrogen metabolism • molecular biology


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