Journal ArticleDOI
NMR studies of hemoproteins: pH dependence of ferric horseradish peroxidase and horse heart myoglobin.
Tetsutaro Iizuka,Satoshi Ogawa,Satoshi Ogawa,Toshiro Inubushi,Toshiro Inubushi,Teijiro Yonezawa,Teijiro Yonezawa,Isao Morishima,Isao Morishima +8 more
TLDR
Measurements of pH-dependence for ferric horseradish peroxidase and horse heart myoglobin covering the large hyperfine shift of heme ring methyl groups due to ferric high spin state confirmed the result of magnetic susceptibility measurements by Theorell and Ehrenberg, and was able to distinguish the nature of the pH dependent spin state change between both hemoproteins.About:
This article is published in FEBS Letters.The article was published on 1976-04-01. It has received 29 citations till now. The article focuses on the topics: Heme & Ferric.read more
Citations
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Journal ArticleDOI
Kinetic and mechanistic studies of the NO*-mediated oxidation of oxymyoglobin and oxyhemoglobin.
TL;DR: This result indicates that, as confirmed from protein analysis after reacting the proteins with NO* for 10 times, when peroxynitrite is coordinated to the heme of myoglobin or hemoglobin it rapidly isomerizes to nitrate without nitrating the globins in physiologically significant amounts.
Journal ArticleDOI
Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line.
Junji Teraoka,T Kitagawa +1 more
TL;DR: It seems rather likely that the proximal histidine is very strongly hydrogen-bonded at both sides of the transition but an appreciable strain is exerted to the Fe-N,(His) bond at the alkaline side presumably due to a conformation change of the polypeptide chain upon ionization of distal histidine.
Journal ArticleDOI
Kinetic and spectroscopic characterization of an intermediate peroxynitrite complex in the nitrogen monoxide induced oxidation of oxyhemoglobin
TL;DR: Kinetic and spectroscopic properties of this intermediate support its assignment as a methemoglobin peroxynitrite complex in the pH range 5–10.5.
Journal ArticleDOI
Resonance Raman spectroscopic evidence for heme iron-hydroxide ligation in peroxidase alkaline forms.
TL;DR: This report provides resonance Raman evidence, using Soret excitation, that alkaline horseradish peroxidase does in fact contain a heme iron-ligated hydroxyl group and observations are rationalized in terms of oxidation of a ligated ferric hydroxide group facilitated through base catalysis by a distal histidine.
References
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Journal ArticleDOI
Spectrophotometric, Magnetic and Titrimetric Studies on the Heme-linked Groups in Myoglobin.
Journal ArticleDOI
Nuclear magnetic resonance evidence for the absence of iron coordinated water in horseradish peroxidase.
Amos Lanir,Abel Schejter +1 more
TL;DR: The pH dependence of longitudinal relaxation rates of water protons in horseradish peroxidase solutions indicates that water is not coordinated to the ferric iron of the enzyme.
Journal ArticleDOI
NMR studies of hemoproteins. VI. Acid-base transitions of ferric myoglobin and its imidazole complex.
Tetsutaro Iizuka,Isao Morishima +1 more
TL;DR: In horse and sperm whale ferric myoglobins, pH-dependent shift of heme-ring methyl signals above p2H 10 was analyzed on the basis of rapid exchange between alkaline and acidic forms, and limiting shifts of three methyl signals were reasonably determined for purely alkaline form.
Journal ArticleDOI
Proton magnetic resonance studies of peroxidases from turnip and horseradish.
TL;DR: Ligand proton resonances have been resolved in spectra of the cyanide complexes of the peroxidases and these provide information on the heme electronic structure.
Journal ArticleDOI
The haem-environment in horseradish peroxidase as seen by proton magnetic relaxation
S. Vuk-Pavlović,B. Benko +1 more
TL;DR: The water-proton fast exchange between the vicinity of the ferric haemiron and bulk solvent in horseradish peroxidase solutions at neutral pH has been directly verified by measuring the proton magnetic relaxation times of the aliphatic protons from ethanediol in an otherwise deuterated solution.
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Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin.
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