Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance Raman scattering

Nagai, Kiyoshi; Kitagawa, Teizo; Morimoto, Hideki

doi:10.1016/0022-2836(80)90374-5

Cited by 226 publications

(134 citation statements)

References 52 publications

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“…Spectra E and F illustrate the differences between spectra A and B, and between spectra C and D, respectively, in which an intense porphyrin band at 678 cm-' was used as a marker for subtraction. A differential pattern exhibiting a peak at 568 cm-' and a trough at 535 cm' appeared in difference spectra E and F. The frequencies 568 cm' for 1602 and 535 cm-' for "02 are in reasonable agreement with the Fe-Os stretching frequencies reported for oxyhemoglobin [27,28], oxymyoglobin [29,30], and dioxygen-bound bovine cytochrome c oxidase [16-18,241. Cryogenic flash/trap absorption experiments on the CO adduct of this enzyme in the presence of oxygen suggested the formation of an oxygenated heme at low temperatures [31].…”

Section: Methodssupporting

confidence: 78%

Observation of the Fe–O₂ and Fe^IV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

et al. 1994

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Reaction intermediates in dioxygen reduction by the E. coli cytochrome bo-type ubiquinol oxidase were studied by time-resolved resonance Raman spectroscopy using the artificial cardiovascular system. At O-20 ps following photolysis of the enzyme-CO adduct in the presence of 0,, we observed the Fe&& stretching Raman band at 568 cm-' which shifted to 535 cm-' with the "0, derivative. These frequencies are remarkably close to those of other oxyhemoproteins including dioxygen-bound hemoglobin and aa,-type cytochrome c oxidase. In the later time range (20-40 ps), other oxygen-isotope-sensitive Raman bands were observed at 788 and 361 cm-'. Since the 781 cm-' band exhibited a downshift by 37 cm-' upon '*O, substitution, we assigned it to the Fe'"=0 stretching mode. This band is considered to arise from the ferry1 intermediate, but its appearance was much earlier than the corresponding intermediate of bovine cytochrome c oxidase (>I00 ps). The 361 cn-' band showed the '60/'s0 isotopic frequency shift of I4 cm-' similar to the case of bovine cytochrome c oxidase reaction.

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Section: Methodssupporting

confidence: 78%

Observation of the Fe–O₂ and Fe^IV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

et al. 1994

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“…Raman lines are also seen in 5-coordinate deoxyhemoglobin [16]. The 220 cm -1 line in deoxyhemoglobin has been shown to result from an imidazoleiron stretching mode [17]. Its presence in the Pseudomonas cytochrome oxidase spectrum is thus consistent with 5-coordination with an imidazole ligand.…”

Section: Resultsmentioning

confidence: 85%

Resonance Raman spectra of heme c and heme d₁ in Pseudomonas cytochrome oxidase

Ching¹,

Ondrias²,

Rousseau³

et al. 1982

FEBS Letters

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“…The RR spectra of the fully reduced [PheP63]Hb exhibit great similarity with those of normal human deoxy Hb excited in the Soret region (Figs. 2 and 3) (Rousseau and Ondrias, 1983;Nagai et al, 1980b: Desbois et al, 1984. In the 1450-1650-cm-' regions of the RR spectra (Fig.…”

Section: Resultsmentioning

confidence: 95%

Recombinant [Pheβ63]Hemoglobin Shows Rapid Oxidation of the β Chains and Low‐Affinity, Non‐Cooperative Oxygen Binding to the α Subunits

Kiger¹,

Baudin²,

Desbois³

et al. 1997

European Journal of Biochemistry

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We have engineered αβ2 [Phe63]hemoglobin by changing the highly conserved distal histidine of the β chains to a phenylalanine. The mutant tetramer binds four high‐affinity ligands, such as CO or NO, to the ferrous form, or CN to the oxidized iron; however, it binds only two low‐affinity ligands, oxygen and azide. The absorption spectrum of the ferrous deoxy or ferric forms are not normal, displaying an enhanced absorption of the visible band near 560 nm. Half of the autooxidation process, attributed to the mutated β subunits, is over 1000‐fold faster than for Hb A. The mutant Hb exhibits non‐cooperative binding of two oxygens with an affinity about fivefold lower than those of HbA valency hybrids (αmetβ)2. Functional properties of this mutant Hb resemble those of Hb Saskatoon ([Tyr63]Hb) [Suzuki, T., Hayashi, A., Shimizu, A. & Yamamura, Y. (1966) Biochim. Biophys. Acta 127, 280–2821, Flash‐photolysis experiments also indicate non‐cooperative behaviour: the CO‐recombination kinetics were independent of the fraction dissociated. Furthermore, the amplitude of the CO bimolecular phase was the same for the (αcometβ), valency hybrid or the (αcoβco), form, suggesting mainly geminate CO‐recombination kinetics to the β chains. EPR and Resonance Raman spectra did not show evidence for a hemichrome, normally considered as a six‐coordinated iron with low‐spin character. The EPR and resonance Raman spectra for the mutated β subunits demonstrate the presence of a high‐spin compound in the ferric and deoxy ferrous forms. In particular, the ferrous mutated β subunits are penta‐coordinated. The abnormal absorption spectra are possibly due to an interaction between the porphyrin and the phenyl ring in the distal position rather than to direct binding to the iron.

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Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance Raman scattering

Cited by 226 publications

References 52 publications

Observation of the Fe–O₂ and Fe^IV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

Observation of the Fe–O₂ and Fe^IV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

Resonance Raman spectra of heme c and heme d₁ in Pseudomonas cytochrome oxidase

Recombinant [Pheβ63]Hemoglobin Shows Rapid Oxidation of the β Chains and Low‐Affinity, Non‐Cooperative Oxygen Binding to the α Subunits

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Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance Raman scattering

Cited by 226 publications

References 52 publications

Observation of the Fe–O2 and FeIV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

Observation of the Fe–O2 and FeIV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

Resonance Raman spectra of heme c and heme d1 in Pseudomonas cytochrome oxidase

Recombinant [Pheβ63]Hemoglobin Shows Rapid Oxidation of the β Chains and Low‐Affinity, Non‐Cooperative Oxygen Binding to the α Subunits

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Observation of the Fe–O₂ and Fe^IV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

Observation of the Fe–O₂ and Fe^IV=O stretching Raman bands for dioxygen reduction intermediates of cytochrome bo isolated from Escherichia coli

Resonance Raman spectra of heme c and heme d₁ in Pseudomonas cytochrome oxidase