Document Detail


The stereospecificity of nitrate reductase for hydrogen removal from reduced pyridine nucleotides.
MedLine Citation:
PMID:  16653     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The stereospecificity of the hydrogen removal from reduced pyridine nucleotides catalyzed by nitrate reductase (NADH : nitrate oxidoreductase, EC 1.6.6.1, and NAD(P)H : nitrate oxidoreductase, EC 1.6.6.2) was investigated. A high degree of enzyme purification was required to obtain conclusive results. Improvements are described for the purification of nitrate reductase from Chlorella fusca and from spinach (Spinacea oleracea, L.) leaves. The latter enzyme is shown to contain a cytochrome. With highly purified nitrate reductase preparations from Cl. fusca, Neurospora crassa, Rhodotorula glutinis and spinach leaves the stereospecificity of the reaction was determined to be predominantly of the A-type in all cases.
Authors:
M G Guerrero; K Jetschmann; W Völker
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  482     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1977 May 
Date Detail:
Created Date:  1977-07-18     Completed Date:  1977-07-18     Revised Date:  2005-11-17    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  19-26     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Chlorella / enzymology
NAD
NADP
Neurospora crassa / enzymology
Nitrate Reductases / isolation & purification,  metabolism*
Oxidation-Reduction
Plants / enzymology
Rhodotorula / enzymology
Species Specificity
Spectrophotometry
Chemical
Reg. No./Substance:
53-59-8/NADP; 53-84-9/NAD; EC 1.7.-/Nitrate Reductases

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