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Mechanism of initial reaction of phenylhydrazine with oxyhemoglobin and effect of ring substitutions on the biomolecular rate constant of this reaction.
TLDR
Phenylhydrazine in the presence of oxygen causes the oxidative denaturation of hemoglobin and is converted to the same complex as that produced when phenyldiazene is added to methemoglobin anaerobically.
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Assessing the hierarchical structure of titanium implant surfaces.
TLDR
The results support recent published studies that show a combination of appropriate micron and nano surface results in a more robust cellular response and increased osteoblast differentiation.
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Formation of aryl and aryldiazenyl complexes in reactions of arylhydrazines and aryldiazenes with a synthetic model compound of haemoprotein.
TLDR
These ligand-binding reactions indicated that the complex of chelated protohaem with phenyldiazene can behave either as a complex of a ferric porphyrin with Phenyldiazenyl anion (C6H5N = N-) or a complex with the visible-absorption spectrum of aFerrihaemochrome.
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Bonding of nitrosobenzene and phenyl isocyanide to chelated mesoheme, hemoglobin and ferrous phthalocyanine.
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Difference in rates of the reaction of various mammalian oxyhemoglobins with phenylhydrazine
TLDR
The results suggest that the reactivity of PHZ to Hb is influenced by the globin molecule, and the oxidative cleavage of the porphyrin ring causes the denaturation of hemoprotein.
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