Results 1 to 10 of about 1,725 (195)
Role of the Circadian Gas-Responsive Hemeprotein NPAS2 in Physiology and Pathology [PDF]
Biology, 2023 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.
Emanuele Murgo +4 more
doaj +7 more sources
Finding Value in Wastewaters from the Cork Industry: Carbon Dots Synthesis and Fluorescence for Hemeprotein Detection [PDF]
Molecules, 2020 Valorisation of industrial low-value waste residues was preconized. Hence, carbon dots (C-dots) were synthesized from wastewaters of the cork industry—an abundant and affordable, but environmentally-problematic industrial effluent.
Marta R. Alexandre +3 more
doaj +3 more sources
Femtosecond imaging of giant-hemeprotein with XFEL pulses.
Biophysical Journal, 2023 Published by Biophysical Soc., Bethesda, Md.
P. Lourdu Xavier +14 more
semanticscholar +4 more sources
Demonstration that spleen green hemeprotein is identical to granulocyte myeloperoxidase.
Journal of Biological Chemistry, 1989 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.
M. Ikeda-Saito +7 more
semanticscholar +5 more sources
How does NO activate hemeproteins? [PDF]
FEBS Letters, 1994 NO was reported to activate guanylate cyclase and, recently, prostaglandin H synthase. NO interaction with the heme component in different hemeproteins is determined by ligand property, electronic configuration of the heme iron and the specific effects contributed by the protein structure.
Ah‐Lim Tsai
openalex +5 more sources
Biomimetic chemistry of hemeproteins.
The Keio Journal of Medicine, 1989 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 ...
David Dolphin
openalex +5 more sources
Open Chemistry, 2020 A unique method was used to synthesize extremely stable silver stearate nanoparticles (AgStNPs) incorporated in an organic-based monolith. The facile strategy was then used to selectively isolate hemeproteins, myoglobin (Myo)
Alzahrani Eman
doaj +2 more sources
Assimilatory Nitrate Reductase of Rhodopseudomonas capsulata AD2: A Molybdo-Hemeprotein [PDF]
Zeitschrift fur Naturforschung. Section C, Biosciences, 1979 The assimilatory nitrate reductase of the phototrophic bacterium Rhodopseudomonas capsulata strain AD2 was purified to homogeneity by a combination of ammonium sulfate fractionation, chromatography on DEAE-cellulose and isoelectric focusing (isoelectric ...
Kasem Alef, J. Klemme
semanticscholar +2 more sources
Mechanism of Sulfide Binding by Ferric Hemeproteins [PDF]
Inorganic Chemistry, 2018 The reaction of hydrogen sulfide (H2S) with hemeproteins is a key physiological reaction; still, its mechanism and implications are not completely understood. In this work, we propose a combination of experimental and theoretical tools to shed light on the reaction in model system microperoxidase 11 (MP11-FeIII) and myoglobin (Mb-FeIII), from the ...
Fernando M. Boubeta +5 more
openalex +5 more sources
Light‐Induced Pulsed EPR Dipolar Spectroscopy on a Paradigmatic Hemeprotein
ChemPhysChem, 2019 Light‐induced pulsed EPR dipolar spectroscopic methods allow the determination of nanometer distances between paramagnetic sites. Here we employ orthogonal spin labels, a chromophore triplet state and a stable radical, to carry out distance measurements ...
Maria Giulia Dal Farra +8 more
semanticscholar +6 more sources