The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach |
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Authors: | Jatindra N. Tripathy Masakazu Hirasawa Sung-Kun Kim Aaron T. Setterdahl James P. Allen David B. Knaff |
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Affiliation: | (1) Department of Chemistry and Biochemistry, Texas Tech University, 1 Circle Drive, Lubbock, TX 79409-1061, USA;(2) Present address: Department of Biology, Indiana University, Bloomington, IN, USA;(3) Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287-1604, USA;(4) Center for Biotechnology and Genomics, Texas Tech University, Lubbock, TX 79409-1061, USA |
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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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Keywords: | Nitrite reductase Ferredoxin Tryptophan |
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