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
Ligand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations. [PDF]
Physical Chemistry, Chemical Physics - PCCP, 2013 The presence of cavities and tunnels in the interior of proteins, in conjunction with the structural plasticity arising from the coupling to the thermal fluctuations of the protein scaffold, has profound consequences on the pathways followed by ligands ...
S. Abbruzzetti +4 more
semanticscholar +2 more sources
Hydrogen peroxide-dependent formation and bleaching of the higher oxidation states of bovine erythrocyte green hemeprotein. [PDF]
Archives of Biochemistry and Biophysics, 1993 The ferric and ferrous forms of bovine erythrocyte green hemeprotein react with hydroperoxides to form higher oxidation state intermediates with absorbance maxima in the Soret region at 426 and 422 nm, respectively.
F. Xu +3 more
semanticscholar +2 more sources
Chemoselective Caging of Carboxyl Groups for On-Demand Protein Activation with Small Molecules. [PDF]
Angew Chem Int Ed Engl, 2023 The caging of amino acid side chains can provide exquisite control of protein function. The first chemical caging of carboxyl groups (Asp and Glu) in enzymic active sites is reported. Caging of a heme propionate in a protein was also feasible by this approach based on esterification with a tuned diazo compound.
Petri YD, Gutierrez CS, Raines RT.
europepmc +3 more sources
Hyperfine correlation spectroscopy and electron spin echo envelope modulation spectroscopy study of the two coexisting forms of the hemeprotein cytochrome c6 from Anabaena Pcc7119. [PDF]
Biophysical Journal, 2009 Oxidized cytochrome c(6) from Anabaena PCC 7119 was studied by electron spin echo envelope modulation spectroscopy. Hyperfine couplings of the unpaired electron with several nuclei were detected, in particular those of the nitrogens bound to the iron ...
I. García‐Rubio +3 more
semanticscholar +2 more sources
Rhabdomyolysis as cause, consequence, or mimicker of myocardial infarction: A case report. [PDF]
Clin Case Rep, 2023 Key Clinical Message A timely diagnosis is essential to start appropriate therapy and to reduce risks of life‐threatening complications of rhabdomyolysis. Some cases can undergo differential diagnosis with other clinical conditions, e.g., myocardial infarction.
Nasello M +11 more
europepmc +2 more sources
Implication to the catalytic process of hemeproteins [PDF]
Acta Crystallographica Section A Foundations of Crystallography, 2011 Y. Ohgo +8 more
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Editorial: Metalloproteins as sensors of gaseous small molecules—From bench to bed and beyond [PDF]
Frontiers in Molecular Biosciences, 2023 Eduardo H. S. Sousa, Shiliang Tian
doaj +2 more sources
Inside Cover: De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four‐Helix Bundle Hemeprotein (Chem. Eur. J. 50/2012) [PDF]
, 2012 M. Faiella +6 more
semanticscholar +2 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
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