Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism.
J R Lancaster,José M. Vega,Henry Kamin,N R Orme-Johnson,William H. Orme-Johnson,Rick J. Krueger,Lewis M. Siegel +6 more
TLDR
EPR spectroscopic and chemical analyses of spinach nitrite reductase show that the enzyme contains one reducible iron-sulfur center, and one site for binding either cyanide or nitrite, per siroheme, indicating a role for the Fe4S4 center in catalysis.About:
This article is published in Journal of Biological Chemistry.The article was published on 1979-02-25 and is currently open access. It has received 111 citations till now. The article focuses on the topics: Ferredoxin—nitrite reductase & Nitrite reductase.read more
Citations
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Journal ArticleDOI
Ferredoxin-dependent chloroplast enzymes.
David B. Knaff,Masakazu Hirasawa +1 more
TL;DR: Article de synthese traitant des proprietes biochimiques and structurales des ferredoxines des cyanobacteries, algues et plantes superieures, en particulier dans les mecanismes d'action des enzymes NADP.
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Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase.
TL;DR: Physicochemical analyses and deduced amino acid sequences indicate that SiR-FP is an octamer of identical 66-kDa peptides and contains 4 FAD and 4 FMN per octamer, and shares a catalytic mechanism with NADPH-cytochrome P-450 oxidoreductase.
Journal ArticleDOI
The isolation of a hexaheme cytochrome from Desulfovibrio desulfuricans and its identification as a new type of nitrite reductase.
Ming-Cheh Liu,Harry D. Peck +1 more
TL;DR: The dithionite-reduced nitrite reductase was demonstrated to be auto-oxidizable even in the presence of potassium cyanide and the difference in Km values seems to exclude the possibility of hydroxylamine being a free intermediate in the reduction of nitrite.
Journal ArticleDOI
Isolation of cDNA clones coding for spinach nitrite reductase: complete sequence and nitrate induction.
TL;DR: The complete primary sequence of the precursor protein for spinach nitrite reductase has been deduced from cloned cDNAs, which most likely serve as a transit peptide involved in directing this nuclearencoded protein into the chloroplast.
References
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Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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Studies on the chemical nature of clostridial ferredoxin.
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The Effects of Protein Conformation on the Heme Symmetry in High Spin Ferric Heme Proteins as Studied by Electron Paramagnetic Resonance
TL;DR: The EPR of high spin heme proteins can be used as a protein conformational probe and the characteristics of the EPR spectrum may be used to describe the symmetry of the heme.
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Reduced Nicotinamide Adenine Dinucleotide Phosphate-Sulfite Reductase of Enterobacteria I. THE ESCHERICHIA COLI HEMOFLAVOPROTEIN: MOLECULAR PARAMETERS AND PROSTHETIC GROUPS
TL;DR: Data indicate that E. coli sulfite reductase is a self-contained complex of electron transport carriers including a heme-type component which, by virtue of its spectrophotometric, solubility, and chromatographic properties, is clearly distinguishable from previously described hemes.
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Paramagnetic resonance study of Nitric Oxide hemoglobin.
TL;DR: Modifying NO-hemoglobin with sodium dodecyl sulfate (SDS) shifted the whole spectrum toward a lower magnetic field retaining the rhombic symmetry, and transformation of the spectrum indicated the randomization of the structure and the change of symmetry type around the paramagnetic center from rhombi to axial.
Related Papers (5)
Spinach nitrite reductase. Purification and properties of a siroheme-containing iron-sulfur enzyme.
José M. Vega,H Kamin +1 more