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J L Matteson

Publications and source records attributed to J L Matteson.

5 recordsLinked to original sources
PubMed1995

Difference in rates of the reaction of various mammalian oxyhemoglobins with phenylhydrazine.

Second order rate constants for the initial reaction of 12 mammalian oxyhemoglobins (Hb) with equimolar phenylhydrazine (PHZ), a compound inducing Heinz body hemolytic anemia, were determined by recording continuous changes in absorbance with time at 577 nm. The rate constants were varied in a range from 43 m-1.s-1 with pig Hb to 255 m-1.s-1 with dog Hb. On the other hand, isosbestic points at 526 and 587 nm were common to all the reaction processes. The aerobic reaction of Hb with PHZ resulted in denaturation of hemoprotein, and final reaction products were determined to be beta-meso-phenylbiliverdin IX alpha and N-phenylprotoporphyrin IX. These 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.

Animals↗
PubMed1988

Bonding of nitrosobenzene and phenyl isocyanide to chelated mesoheme, hemoglobin and ferrous phthalocyanine.

Reactions of nitrosobenzene, phenyl isocyanide and their ring-substituted analogues with hemoglobin, ferrous phthalocyanine and a synthetic model compound of hemoglobin were investigated by optical, 1H-NMR and infrared spectroscopy. Complexes of chelated ferromesoheme, the model compound, with 2-methyl-, 2-ethyl, 2-isopropyl- or 2,6-disubstituted nitrosobenzene were less stable than its complex with nitrosobenzene. Formation of a complex of the model compound with 2-tert-butylnitrosobenzene was incomplete. Previous studies showed that 2,6-disubstituted nitrosobenzenes are not ligands of ferrohemoglobin. In the present work 2,6-dimethylphenyl isocyanide was found to be a ligand of ferrohemoglobin. These results are consistent with binding of the nitrogen of the nitroso group of nitrosobenzene and of the carbon of the isocyanide group of phenyl isocyanide to ferroheme. The same bonding modes of these ligands to ferrous phthalocyanine were inferred from ring-current-induced shifts in the 1H-NMR spectra of the respective complexes.

Chlorides↗
PubMed1986

Formation of aryl and aryldiazenyl complexes in reactions of arylhydrazines and aryldiazenes with a synthetic model compound of haemoprotein.

The anaerobic reaction of chelated protohaemin, a synthetic model compound of ferrihaemoglobin, with phenyldiazene produced a compound with the visible-absorption spectrum of a ferrihaemochrome. The compound reacted with CN-, which is a ligand of both ferric and ferrous porphyrins, to produce the complex of the synthetic ferrihaemoglobin with CN-. Though the spectrum of the compound formed by the addition of phenyldiazene to chelated protohaemin is characteristic of a ferric porphyrin complex, this compound reacted with both toluene-p-sulphonylmethyl isocyanide and CO, which are strong ligands of ferrous porphyrins, to produce the corresponding ferrous complexes. 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 of a ferrous porphyrin with phenyldiazenyl radical (C6H5N = N.). Para substituents on phenyldiazene were without effect on the formation of 4-substituted phenyldiazenyl complexes with chelated protohaem. Ortho substituents resulted in less-stable complexes. The phenyl complex of chelated protohaem was prepared by the aerobic reaction of phenylhydrazine with chelated protohaemin, and its structure was confirmed by its n.m.r. spectrum. The ligand-binding properties, n.m.r. spectrum and absorption spectrum of this complex differed from those of the phenyldiazenyl complex. The phenyl complex also was produced when the phenyldiazenyl complex was exposed to O2.

Carbon Monoxide↗
PubMed1982

Mechanism of initial reaction of phenylhydrazine with oxyhemoglobin and effect of ring substitutions on the biomolecular rate constant of this reaction.

Phenylhydrazine in the presence of oxygen causes the oxidative denaturation of hemoglobin. The initial step in this process is a bimolecular reaction, probably a two-electron transfer from phenylhydrazine to oxyhemoglobin. The product of this reaction is neither methemoglobin nor deoxyhemoglobin. Superoxide dismutase and catalase eliminate side reactions that increase the apparent rate of this reaction as measured spectrophotometrically at 577 nm; scavengers for the hydroxyl radical and singlet oxygen do not affect this rate either in the presence or in the absence of these enzymes. Halogen atoms and alkyl groups decrease the rate when ortho and increase the rate when meta or para to the hydrazino group. Chlorine atoms at both ortho positions or the carboxylate group at the ortho or the para position block the reaction. In the presence of phenylhydrazine under air, methemoglobin is converted to the same complex as that produced when phenyldiazene is added to methemoglobin anaerobically. Under N2 or CO, phenylhydrazine reduces methemoglobin to deoxyhemoglobin or carbonmonoxyhemoglobin.

Catalase↗