Assignment of the Fe—Nϵ (His F8) stretching band in the resonance Raman spectra of deoxy myoglobin
TLDR
In this paper, the resonance Raman spectrum (RRS) of deoxy myoglobin (Mb) in the lowest frequency region was investigated, in which the Fe-N, (His) stretching frequency provided an important insight into molecular mechanism of biolo&al reactions catalyzed by the enzyme.About:
This article is published in FEBS Letters.The article was published on 1979-08-15 and is currently open access. It has received 186 citations till now. The article focuses on the topics: Resonance & Raman spectroscopy.read more
Citations
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Journal ArticleDOI
Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase.
Shin-ichi Adachi,Shingo Nagano,Koichiro Ishimori,Yoshihito Watanabe,Isao Morishima,Tsuyoshi Egawa,Teizo Kitagawa,Ryu Makino +7 more
TL;DR: Histidine-93(F8) in human myoglobin (Mb), which is the proximal ligand of the heme iron, has been replaced with cysteine or tyrosine by site-directed mutagenesis and exhibit the altered axial ligation analogous to P-450, chloroperoxidase, and catalase.
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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.
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CO as a vibrational probe of heme protein active sites.
TL;DR: Carbon monoxide is a useful vibrational probe of heme binding sites in proteins, because FeCO backbonding is modulated by polar interactions with protein residues, and by variations in the donor strength of the trans ligand.
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Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance Raman scattering
TL;DR: It is proposed that the 216 cm−1 line of deoxy Hb is associated primarily with the FeNe(HisF8) stretching mode and accordingly that the Fe £1,000,000 bond is stretched in the T state due to a strain exerted by globin.
References
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Stereochemistry of cooperative effects in haemoglobin.
TL;DR: The oxygenation of haemoglobin is accompanied by structural changes in the subunits triggered by shifts of the iron atoms relative to the porphyrin and, in the β-subunits, also by the steric effect of oxygen itself.
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Three-dimensional fourier synthesis of calf liver cytochrome b5 at 2.8 Å resolution
TL;DR: The electron density of calf liver cytochrome b5 has been calculated to a resolution of 2.8 A and the phases of the 2500 Fourier coefficients were determined by the isomorphous replacement method using two derivatives, mersalyl and uranyl acetate.
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Preparation of crystalline oxymyoglobin from horse heart.
TL;DR: This communication deals with procedures for the isolation of native oxy myoglobin from fresh horse heart, and the chromatographic separation of oxymyoglobin from metmyoglobin with diethylaminoethyl cellulose.
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Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modes.
TL;DR: Mechanisms for the resonance enhancement of the main low-frequency bands are discussed on the basis of the excitation profiles and of the dispersion curves for depolarization ratios obtained for fluorometmyoglobin and hydroxymetmyoglobin.
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Studies on Cytochrome c Peroxidase XII. CRYSTALLINE SYNTHETIC ENZYMES CONTAINING UNNATURAL HEME PROSTHETIC GROUPS
Takashi Yonetani,Toshio Asakura +1 more
TL;DR: The enzymic activities of these synthetic enzymes in the peroxidatic oxidation offerrocytochrome c, ferrocyanide, and ascorbate were found to be quite similar, indicating that the side chains of porphyrin IX at positions 2 and 4 were not essential for the catalytic activity of cy tochrome c peroxIDase.
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Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance Raman scattering
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Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line.
Junji Teraoka,T Kitagawa +1 more