Results 21 to 30 of about 1,715 (116)
Role of the Circadian Gas-Responsive Hemeprotein NPAS2 in Physiology and Pathology
Neuronal PAS domain protein 2 (NPAS2) is a hemeprotein comprising a basic helix–loop–helix domain (bHLH) and two heme-binding sites, the PAS-A and PAS-B domains. This protein acts as a pyridine nucleotide-dependent and gas-responsive CO-dependent transcription factor and is encoded by a gene whose expression fluctuates with circadian rhythmicity. NPAS2
Emanuele Murgo+4 more
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Heme on innate immunity and inflammation
Heme is an essential molecule expressed ubiquitously all through our tissues. Heme plays major functions in cellular physiology and metabolism as the prostetic group of diverse proteins.
Fabianno Ferreira Dutra+1 more
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Biomimetic chemistry of hemeproteins.
Hemeproteins play important physiological roles for an oxygen metabolism in living organisms. Their functions are divided to three main groups, i) hemoglobins, myoglobins and the cytochromes which function by transporting and storing dioxygen and electrons; ii) catalase and peroxidases which are activated by hydrogen peroxide, iii) cytochrome oxidase ...
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Hydrogen sulfide activation in hemeproteins: The sulfheme scenario [PDF]
Traditionally known as a toxic gas, hydrogen sulfide (H2S) is now recognized as an important biological molecule involved in numerous physiological functions. Like nitric oxide (NO) and carbon monoxide (CO), H2S is produced endogenously in tissues and cells and can modulate biological processes by acting on target proteins.
Juan López-Garriga+3 more
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Background Phanerochaete chrysosporium, the model white rot basidiomycetous fungus, has the extraordinary ability to mineralize (to CO2) lignin and detoxify a variety of chemical pollutants.
Yadav Jagjit S+2 more
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Nitric Oxide Binding Geometry in Heme-Proteins: Relevance for Signal Transduction
Nitric oxide (NO) synthesis, signaling, and scavenging is associated to relevant physiological and pathological events. In all tissues and organs, NO levels and related functions are regulated at different levels, with heme proteins playing pivotal roles.
Giovanna De Simone+4 more
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Influence of the freezing process upon fluoride binding to hemeproteins [PDF]
Fluoride association with ferric myoglobins and hemoglobins in aqueous buffers above freezing has been well studied. We chose this reaction to investigate the feasibility of observing titration intermediates and estimating dissociation constants at the freezing temperature by electron paramagnetic resonance spectroscopy at cryogenic temperatures ...
An-Suei Yang, Arthur S. Brill
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Mechanistics of pH-Dependent Sulfmyoglobin Formation: Spin Control and His64 Proton Relay
The chemistry of hydrogen sulfide (H2S) has been directed towards physiologically relevant hemeproteins, including myoglobin, hemoglobin, and other similar proteins.
Angel D. Rodriguez-Mackenzie+4 more
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Demonstration that spleen green hemeprotein is identical to granulocyte myeloperoxidase
The biochemical, spectroscopic, enzymatic, and redox properties of spleen myeloperoxidase, a peroxidase formerly called "spleen green hemeprotein," and granulocyte myeloperoxidase were compared by electrophoresis, amino-terminal amino acid sequences, optical and EPR spectroscopy, steady-state enzyme kinetics, and oxidation-reduction potential.
R C Prince+7 more
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Genetic Polymorphisms in CYP2 Gene Family in Bulgarian Individuals and their Clinical Implications
The cytochrome P450 superfamily consists of hemeproteins involved in the detoxication of different xenobiotics, including drugs. The CYP2 gene family is responsible for the metabolism of 80% of the drugs in clinical use.
Yovinska S.+6 more
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