Identification of the iron-ligand vibration of oxyhemoglobin

Brunner, H.

doi:10.1007/bf00606289

Cited by 119 publications

(52 citation statements)

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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: 76%

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: 76%

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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“…17 In follow-up work, Brunner used an oxygen isotope to identify a mode assignable to stretching of the iron-oxygen (Fe-O 2 ) bond at 567 cm À1 (Figure 2). 18 Understanding the nature of the Fe-O 2 bond was thought to be vital to the elucidation of oxygen binding in hemoglobin, and it became the subject of much research. In 1973, Yamamoto et al studied different forms of hemoglobin protein with RRS (441.6 nm excitation) to deduce the nature of the Fe-O 2 bond in oxyHb.…”

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confidence: 99%

Raman Spectroscopy of Blood and Blood Components

et al. 2017

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Blood is a bodily fluid that is vital for a number of life functions in animals. To a first approximation, blood is a mildly alkaline aqueous fluid (plasma) in which a large number of free-floating red cells (erythrocytes), white cells (leucocytes), and platelets are suspended. The primary function of blood is to transport oxygen from the lungs to all the cells of the body and move carbon dioxide in the return direction after it is produced by the cells' metabolism. Blood also carries nutrients to the cells and brings waste products to the liver and kidneys. Measured levels of oxygen, nutrients, waste, and electrolytes in blood are often used for clinical assessment of human health. Raman spectroscopy is a nondestructive analytical technique that uses the inelastic scattering of light to provide information on chemical composition, and hence has a potential role in this clinical assessment process. Raman spectroscopic probing of blood components and of whole blood has been on-going for more than four decades and has proven useful in applications ranging from the understanding of hemoglobin oxygenation, to the discrimination of cancerous cells from healthy lymphocytes, and the forensic investigation of crime scenes. In this paper, we review the literature in the field, collate the published Raman spectroscopy studies of erythrocytes, leucocytes, platelets, plasma, and whole blood, and attempt to draw general conclusions on the state of the field.

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“…Indeed, if the Co-N-0 bond angle is < 180" there is a certain mixing between stretching and bending modes. Interestingly, this isotope-sensitive line at 573 cm-' is identical to the Fe-02 stretching frequency in oxy sperm whale myoglobin [3] and is very close to 567 cm-' found and assigned originally by Brunner in Hb A [2].…”

Section: Assignment Of Co-no Stretching Mode In Cobalt Hemoglobinsmentioning

confidence: 57%

“…Therefore, the nitrosylated cobalt hemoglobins are of particular interest for investigating the interactions of the exogenous ligand with the protein side groups on the distal side of the heme. Since the Fe-02 stretching vibration has been first observed by Brunner in oxy Hb A [2] and later by other authors in many hemoglobins , it is of particular interest to find the corresponding Co-NO stretching frequency. The assignment of the CO-NO stretching mode is easier than that of the v(Fe-02) as various isotopically labelled nitric oxides (14N'60,'5N'60, 14N'80) are available.…”

mentioning

confidence: 99%

The cobalt‐nitrosyl stretching vibration as a sensitive resonance Raman probe for distal histidine‐nitrosyl interaction in monomeric hemoglobins

Thompson

Mizukami

et al. 1986

European Journal of Biochemistry

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The Co-NO stretching vibration has been assigned in the resonance Raman spectra of various cobaltMonomeric hemoglobins with a distal histidine (sperm whale myoglobin and leghemoglobin) exhibit this vibration at 573 -575 cm-', whereas hemoglobins without distal histidine (elephant myoglobin and insect hemoglobin from Chironomus thummi thummi, CTT 111) show this vibration in the range of 553 -558 cm-'. The Fe-NO stretching vibration which occurs in the range of 554-556 cm-' does not reflect the distal histidine-ligand interaction. Therefore, the Co-NO moiety which is isoelectronic with the Fe-02 moiety is a good monitor for distal effects on the exogenous ligand of hemoglobins, especially due to the fact that in hemoglobins with distal histidine the Fe-02 stretching vibration (567-572 cm-') is similar to the Co-NO stretching vibration.substituted monomeric hemoglobins by employing isotope-labeling of nitrosyl (14N160, 15N160 , 14~180).Cobalt-substituted hemes are capable of binding nitric oxide in the presence of nitrogen bases [l]. The cobalt-nitrosyl moiety is isoelectronic with the iron-dioxygen moiety. It is demonstrated in t h s paper that cobalt-substituted hemoglobins also bind nitric oxide. Therefore, the nitrosylated cobalt hemoglobins are of particular interest for investigating the interactions of the exogenous ligand with the protein side groups on the distal side of the heme. Since the Fe-02 stretching vibration has been first observed by Brunner in oxy Hb A [2] and later by other authors in many hemoglobins [3-61, it is of particular interest to find the corresponding Co-NO stretching frequency. The assignment of the CO-NO stretching mode is easier than that of the v(Fe-02) as various isotopically labelled nitric oxides (14N'60,'5N'60, 14N'80) are available. By comparison of the stretching vibrations of the Co-NO and Fe-02 bonds we can determine the similarities or differences between the metal-ligand bonding interactions in these isoelectronic systems.Four cobalt-substituted monomeric hemoglobins were studied via resonance Raman spectroscopy: sperm whale myoglobin, leghemoglobin from soybean, insect hemoglobin from Chironomus thummi thummi (CTT 111) and elephant myoglobin. These hemoglobins contain the same protoheme-IX as prosthetic groups but they are different with regard to their heme pockets. Thus, we expect that the pophyrin-protein or ligand-protein interactions are different in these hemoglobins. Sperm whale myoglobin has a distal histidine [7], whereas in elephant myoglobin this histidine is replaced by glutamine [S, 91. In CTT 111, the 'distal' hstidine is turned to the surface of the molecule and is thus incapable of interacting MATERIALS AND METHODSSperm whale myoglobin was purchased from Sigma Chemicals (St Louis, MO) and further purified as already described [ 131. Elephant myoglobin [S], leghemoglobin from soybean [14], and CTT 111 from Chironomus thummi thummi [15,16] were purified as described elsewhere. The preparation of cobaltous protoporphyrin-IX and the reconstitution of hemo...

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Identification of the iron-ligand vibration of oxyhemoglobin

Cited by 119 publications

References 5 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

Raman Spectroscopy of Blood and Blood Components

The cobalt‐nitrosyl stretching vibration as a sensitive resonance Raman probe for distal histidine‐nitrosyl interaction in monomeric hemoglobins

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Identification of the iron-ligand vibration of oxyhemoglobin

Cited by 119 publications

References 5 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

Raman Spectroscopy of Blood and Blood Components

The cobalt‐nitrosyl stretching vibration as a sensitive resonance Raman probe for distal histidine‐nitrosyl interaction in monomeric hemoglobins

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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