Document Detail

The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach.
MedLine Citation:
PMID:  17611813     Owner:  NLM     Status:  MEDLINE    
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.
Jatindra N Tripathy; Masakazu Hirasawa; Sung-Kun Kim; Aaron T Setterdahl; James P Allen; David B Knaff
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2007-07-05
Journal Detail:
Title:  Photosynthesis research     Volume:  94     ISSN:  0166-8595     ISO Abbreviation:  Photosyn. Res.     Publication Date:  2007 Oct 
Date Detail:
Created Date:  2007-08-21     Completed Date:  2007-12-28     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100954728     Medline TA:  Photosynth Res     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1-12     Citation Subset:  IM    
Department of Chemistry and Biochemistry, Texas Tech University, 1 Circle Drive, Lubbock, TX 79409-1061, USA.
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MeSH Terms
Circular Dichroism
Ferredoxins / chemistry,  metabolism*
Models, Molecular
Nitrite Reductases / chemistry*,  genetics,  metabolism*
Protein Structure, Tertiary
Spinacia oleracea / enzymology*
Tryptophan / genetics,  metabolism*
Reg. No./Substance:
0/Ferredoxins; 73-22-3/Tryptophan; EC 1.7.-/Nitrite Reductases

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