Electromagnetic Properties of Hemoproteins III. ELECTRON PARAMAGNETIC RESONANCE CHARACTERISTICS OF IRON (III) AND MANGANESE (II) PROTOPORPHYRINS IX AND THEIR APOHEMOPROTEIN COMPLEXES IN HIGH SPIN STATES
Takashi Yonetani,Henry R. Drott,John S. Leigh,George H. Reed,Michael R. Waterman,Toshio Asakura +5 more
TLDR
The combination of metalloporphyrins to apohemoproteins appeared to be an excellent method of achieving an ideal magnetic dilution of paramagnetic centers for EPR studies.About:
This article is published in Journal of Biological Chemistry.The article was published on 1970-06-10 and is currently open access. It has received 69 citations till now. The article focuses on the topics: Electron paramagnetic resonance & Manganese.read more
Citations
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Journal ArticleDOI
Electromagnetic properties of hemoproteins. V. Optical and electron paramagnetic resonance characteristics of nitric oxide derivatives of metalloporphyrin-apohemoprotein complexes.
TL;DR: EPR parameters of nitric oxide complexes of ferrous hemoproteins are not significantly affected by substitutions of two vinyl groups at positions 2 and 4 of the porphyrin ring with two ethyl groups (mesoheme) or hydrogens (deuteroheme), indicating that the nucleophilicity of porphirin side chains has no appreciable effect on the metal-ligand bond strength.
Journal ArticleDOI
The Effects of Protein Conformation on the Heme Symmetry in High Spin Ferric Heme Proteins as Studied by Electron Paramagnetic Resonance
TL;DR: The EPR of high spin heme proteins can be used as a protein conformational probe and the characteristics of the EPR spectrum may be used to describe the symmetry of the heme.
Book ChapterDOI
Preparation and properties of apohemoglobin and reconstituted hemoglobins.
TL;DR: This chapter describes the procedures for the isolation of Globin in the native state and for its reconstitution with metalloporphyrins and presents the physicochemical properties of globin.
Journal ArticleDOI
Studies on cobalt myoglobins and hemoglobins. I. Preparation and optical properties of myoglobins and hemoglobins containing cobalt proto-, meso-, and deuteroporphyrins and thermodynamic characterization of their reversible oxygenation.
TL;DR: Thermochemical comparison of oxygenation parameters of iron- and cobalt-containing oxygen carriers indicates that the effect of the metal substitution on the oxygen affinity is primarily enthalpic, whereas theeffect of the apoprotein binding on theoxy affinity of cobaltous porphyrins is essentially entropic.
References
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Journal ArticleDOI
Studies on cytochrome c peroxidase. I. Purification and some properties.
Takashi Yonetani,Gisela S. Ray +1 more
Journal ArticleDOI
Studies on Cytochrome c Peroxidase: X. CRYSTALLINE APO- AND RECONSTITUTED HOLOENZYMES
TL;DR: The minimum acidity required for the cleavage of the heme-protein link by Teale's acid butanone method was determined for several ferric protohemoproteins and apoenzyme was crystallized as large prisms which may be suitable for physical measurements of single crystals.
Journal ArticleDOI
The Electronic Structure of Protoheme Proteins I. AN ELECTRON PARAMAGNETIC RESONANCE AND OPTICAL STUDY OF HORSERADISH PEROXIDASE AND ITS DERIVATIVES
William E. Blumberg,William E. Blumberg,J. Peisach,J. Peisach,Beatrice A. Wittenberg,Beatrice A. Wittenberg,Jonathan B. Wittenberg,Jonathan B. Wittenberg +7 more
TL;DR: Optical spectra of both Compound I and Compound II of horseradish peroxidase change little with temperature, indicating that neither of these compounds is an equilibrium mixture of species whose relative abundance is affected by temperature.
Journal ArticleDOI
Electron Spin Resonance of High‐Spin d5 Systems
R. D. Dowsing,J. F. Gibson +1 more
TL;DR: In this paper, the electron spin resonance spectra of polycrystalline samples of some sideramines (coprogen, ferrichrysin, ferricrocin, and ferrirubin), transferrin, and conalbumin are reported both at 9.3 and 36 kMc/sec and at various temperatures.
Related Papers (5)
Studies on cytochrome c peroxidase. XV. Comparison of manganese porphyrin-containing cytochrome c peroxidase, horseradish peroxidase, and myoglobin.
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B. M. Hoffman,D. H. Petering +1 more