Hemeproteins

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  Subject Areas on Research

  • A genetic analysis of nitrosative stress. 
  • Activated conformers of Escherichia coli sulfite reductase heme protein subunit. 
  • Alkaline low spin form of sulfite reductase hemeprotein subunit. 
  • Biochemistry of soluble guanylate cyclase. 
  • Biological chemistry of carbon monoxide. 
  • Carbon monoxide binding by simple heme proteins under photodissociating conditions. 
  • Carbon monoxide, reactive oxygen signaling, and oxidative stress. 
  • Carbon monoxide-driven reduction of ferric heme and heme proteins. 
  • Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase. 
  • Compartmentalized nitrosation and nitration in mitochondria. 
  • Differential regulation of beta-chemokines in children with Plasmodium falciparum malaria. 
  • Electron acceptor function of O2 in radical N-demethylation reactions catalyzed by hemeproteins. 
  • Electron paramagnetic resonance and optical spectroscopic evidence for interaction between siroheme and Fe4S4 prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit. 
  • Elevated nitric oxide production in children with malarial anemia: hemozoin-induced nitric oxide synthase type 2 transcripts and nitric oxide in blood mononuclear cells. 
  • Engineered modular recombinant transporters: application of new platform for targeted radiotherapeutic agents to alpha-particle emitting 211 At. 
  • Enzymes that counteract nitrosative stress promote fungal virulence. 
  • Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes. 
  • Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen. 
  • Heme proteins and nitric oxide (NO): the neglected, eloquent chemistry in NO redox signaling and regulation. 
  • Intraleucocyte malaria pigment in asymptomatic and uncomplicated malaria. 
  • Intraleucocytic malaria pigment and clinical severity of malaria in children. 
  • Is the flavohemoglobin a nitric oxide dioxygenase? 
  • Maintenance of nitric oxide and redox homeostasis by the salmonella flavohemoglobin hmp. 
  • Malarial pigment-dependent error in the estimation of hemoglobin content in Plasmodium falciparum-infected red cells: implications for metabolic and biochemical studies of the erythrocytic phases of malaria. 
  • Nitrosative stress: metabolic pathway involving the flavohemoglobin. 
  • On the reaction of ferric heme proteins with nitrite and sulfite. 
  • Oxygen toxicity and iron accumulation in the lungs of mice lacking heme oxygenase-2. 
  • Preliminary X-ray diffraction studies on the hemoprotein subunit of Escherichia coli sulfite reductase. 
  • Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products. 
  • Protection from nitrosative stress by yeast flavohemoglobin. 
  • Protection from nitrosative stress: a central role for microbial flavohemoglobin. 
  • Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands. 
  • Proton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit. 
  • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow. 
  • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein: subunit structure and dissociation into hemoprotein and flavoprotein components. 
  • 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. 
  • 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. 
  • Reduced peripheral PGE2 biosynthesis in Plasmodium falciparum malaria occurs through hemozoin-induced suppression of blood mononuclear cell cyclooxygenase-2 gene expression via an interleukin-10-independent mechanism. 
  • Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes. 
  • Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes. 
  • Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes. 
  • Siroheme and sirohydrochlorin. The basis for a new type of porphyrin-related prosthetic group common to both assimilatory and dissimilatory sulfite reductases. 
  • Siroheme: a new prosthetic group participating in six-electron reduction reactions catalyzed by both sulfite and nitrite reductases. 
  • Spectroelectrochemistry of heme proteins: effects of active-site heterogeneity on Nernst plots. 
  • Suppression of prostaglandin E2 by malaria parasite products and antipyretics promotes overproduction of tumor necrosis factor-alpha: association with the pathogenesis of childhood malarial anemia. 
  • The indispensability of heme oxygenase-1 in protecting against acute heme protein-induced toxicity in vivo.