Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
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Production of β-apo-10'-carotenal from β-carotene by human β-carotene-9',10'-oxygenase expressed in E. coliStabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthaseMetals, oxidative stress and neurodegeneration: a focus on iron, manganese and mercuryA hydrogen-bonding network formed by the B10-E7-E11 residues of a truncated hemoglobin from Tetrahymena pyriformis is critical for stability of bound oxygen and nitric oxide detoxificationDiatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa.Molecular controls of the oxygenation and redox reactions of hemoglobinDifferential sensitivities of pulmonary and coronary arteries to hemoglobin-based oxygen carriers and nitrovasodilators: study in a bovine ex vivo model of vascular strips.Exploring the mechanisms of the reductase activity of neuroglobin by site-directed mutagenesis of the heme distal pocketMolecular biosensing mechanisms in the spleen for the removal of aged and damaged red cells from the blood circulationProtein oxidation mediated by heme-induced active site conversion specific for heme-regulated transcription factor, iron response regulatorSequestration and scavenging of iron in infection.Effective intermediate-spin iron in O2-transporting heme proteins.Iron chemistry at the service of life.Interaction of apoNeuroglobin with heme-Aβ complexes relevant to Alzheimer's disease.Protein-based blood substitutes: recent attempts at controlling pro-oxidant reactivity with and beyond hemoglobin.Iron restriction increases myoglobin gene and protein expression in Soleus muscle of rats.Exploring the Strength of the H-Bond in Synthetic Models for Heme Proteins: The Importance of the N-H Acidity of the Distal Base.Functionalization of nanostructured cerium oxide films with histidine.Rebinding dynamics of NO to microperoxidase-8 probed by time-resolved vibrational spectroscopy.The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
P2860
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P2860
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
@ast
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
@en
type
label
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
@ast
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
@en
prefLabel
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
@ast
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
@en
P1476
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
@en
P2093
Keiji Shikama
P304
P356
10.1016/J.PBIOMOLBIO.2005.04.001
P577
2005-06-09T00:00:00Z