1.8.1.2 A new type of sulfite reductase, a novel coenzyme F420-dependent enzyme, from the methanarchaeon Methanocaldococcus jannaschii Methanocaldococcus jannaschii 1.8.1.2 Activated conformers of Escherichia coli sulfite reductase heme protein subunit [published erratum appears in Biochemistry 1988 Dec 27;27(26):9226] Escherichia coli 1.8.1.2 Characterization of a thermolabile sulfite reductase from Salmonella pullorum Salmonella enterica subsp. enterica serovar Pullorum 1.8.1.2 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 Escherichia coli 1.8.1.2 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 Salmonella enterica subsp. enterica serovar Typhimurium 1.8.1.2 Cloning and characterization of the gene coding for NADPH-sulfite reductase hemoprotein from Actinobacillus pleuropneumoniae and use of the protein product as a vaccine Actinobacillus pleuropneumoniae 1.8.1.2 Cloning of the 3-phosphoadenylyl sulfate reductase and sulfite reductase genes from Escherichia coli K-12 Escherichia coli 1.8.1.2 Enzymatic synthesis of gold nanoparticles using sulfite reductase purified from Escherichia coli A green eco-friendly approach Escherichia coli 1.8.1.2 Enzymatic synthesis of gold nanoparticles using sulfite reductase purified from Escherichia coli A green eco-friendly approach Escherichia coli PTCC 1330 1.8.1.2 Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes Escherichia coli 1.8.1.2 Expression, purification and characterization of the sulfite reductase hemo-subunit, SiR-HP, from Acidithiobacillus ferrooxidans Acidithiobacillus ferrooxidans 1.8.1.2 Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli Escherichia coli 1.8.1.2 Four Crystal Structures of the 60 kDa Flavoprotein Monomer of the Sulfite Reductase Indicate a Disordered Flavodoxin-like Module Escherichia coli 1.8.1.2 Furfural inhibits growth by limiting sulfur assimilation in ethanologenic Escherichia coli strain LY180 Escherichia coli 1.8.1.2 Furfural inhibits growth by limiting sulfur assimilation in ethanologenic Escherichia coli strain LY180 Escherichia coli LY180 1.8.1.2 Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans Cryptococcus deneoformans 1.8.1.2 Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans Cryptococcus deneoformans ATCC MYA-565 1.8.1.2 Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans Cryptococcus deneoformans JEC21 1.8.1.2 Isolation of sulfite reductase variants of a commercial wine yeast with significantly reduced hydrogen sulfide production Saccharomyces cerevisiae 1.8.1.2 Metal-containing flavoprotein dehydrogenases Escherichia coli 1.8.1.2 Metal-containing flavoprotein dehydrogenases Salmonella enterica subsp. enterica serovar Typhimurium 1.8.1.2 Metal-containing flavoprotein dehydrogenases Saccharomyces cerevisiae 1.8.1.2 Metal-containing flavoprotein dehydrogenases Neurospora crassa 1.8.1.2 Molecular cloning of the cys genes (cysC, cysD, cysH, cysI, cysJ, and cysG) responsible for cysteine biosynthesis in Escherichia coli K-12 Escherichia coli 1.8.1.2 NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase Escherichia coli 1.8.1.2 NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction Escherichia coli 1.8.1.2 NADPH-Sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase Escherichia coli 1.8.1.2 Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride Escherichia coli 1.8.1.2 Preliminary X-ray diffraction studies on the hemoprotein subunit of Escherichia coli sulfite reductase Escherichia coli 1.8.1.2 Purification and characterization of Escherichia coli sulfite reductase and its application in surimi processing Escherichia coli 1.8.1.2 Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow Escherichia coli 1.8.1.2 Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups Escherichia coli 1.8.1.2 Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. II. Identification of a new class of heme prosthetic group: an iron-tetrahydroporphyrin (isobacteriochlorin type) with eight carboxylic acid groups Escherichia coli 1.8.1.2 Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein: subunit structure and dissociation into hemoprotein and flavoprotein components Escherichia coli 1.8.1.2 Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. V. Studies with the Escherichia coli hemoflavoprotein depleted of flavin mononucleotide: distinct roles for the flavin adenine dinucleotide and flavin mononucleotide prosthetic groups in catalysis Escherichia coli 1.8.1.2 Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. VI. The reaction of carbon monoxide with the Escherichia coli holoenzyme, the hemoprotein, and free siroheme Escherichia coli 1.8.1.2 Siroheme and sirohydrochlorin. The basis for a new type of porphyrin-related prosthetic group common to both assimilatory and dissimilatory sulfite reductases Desulfotomaculum nigrificans 1.8.1.2 Sirohydrochlorin. Prosthetic group of sulfite and nitrite reductases and its role in the biosynthesis of vitamin B12 Propionibacterium freudenreichii subsp. shermanii 1.8.1.2 Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase Escherichia coli 1.8.1.2 Structure-function relationships in the oligomeric NADPH-dependent assimilatory sulfite reductase Escherichia coli 1.8.1.2 Studies on yeast sulfite reductase. 3. Further characterization Saccharomyces cerevisiae 1.8.1.2 Studies on yeast sulfite reductase. I. Purification and characterization Saccharomyces cerevisiae 1.8.1.2 Studies on yeast sulfite reductase. II. Partial purification and properties of genetically incomplete sulfite reductases Saccharomyces cerevisiae 1.8.1.2 Studies on yeast sulfite reductase. IV. Structure and steady-state kinetics Saccharomyces cerevisiae 1.8.1.2 Studies on yeast sulfite reductase. V. Effects of ionic strength on enzyme activities Saccharomyces cerevisiae 1.8.1.2 Studies on yeast sulfite reductase. VI. Use of the effects of ionic strength as a probe for enzyme structure and mechanism Saccharomyces cerevisiae 1.8.1.2 Sulfite formation by wine yeasts III. Properties of sulfite reductase. Saccharomyces cerevisiae 1.8.1.2 Sulfite formation by wine yeasts III. Properties of sulfite reductase. Saccharomyces bayanus 1.8.1.2 Sulfite reductase (bakers¦ yeast) Saccharomyces cerevisiae 1.8.1.2 Sulphite reductase from bakers yeast: a haemoflavoprotein Saccharomyces cerevisiae 1.8.1.2 The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metalated sirohemes and S = 9/2 iron-sulfur clusters Desulfosarcina variabilis 1.8.1.2 The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis Escherichia coli 1.8.1.2 The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase Escherichia coli 1.8.1.2 The N-terminal domain of Escherichia coli assimilatory NADPH-sulfite reductase hemoprotein is an oligomerization domain that mediates holoenzyme assembly Escherichia coli 1.8.1.2 The NADPH:sulfite reductase of Escherichia coli is a paraquat reductase Escherichia coli 1.8.1.2 The role of extended Fe4S4 cluster ligands in mediating sulfite reductase hemoprotein activity Escherichia coli 1.8.1.2 The role of extended Fe4S4 cluster ligands in mediating sulfite reductase hemoprotein activity Escherichia coli K12 1.8.1.2 TPNH-Sulfite reductase (Escherichia coli) Escherichia coli 1.8.1.2 Ultradian metabolic oscillation of Saccharomyces cerevisiae during aerobic continuous culture: hydrogen sulphide, a population synchronizer, is produced by sulphite reductase Saccharomyces cerevisiae