Resonance Raman scattering on the haem group of oxy- and deoxyhaemoglobin

Brunner, H.; Mayer, A.; Sussner, H.

doi:10.1016/0022-2836(72)90169-6

Cited by 103 publications

(49 citation statements)

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“…It was therefore inferred that these modes were dependent on the displacement between the iron atom and the porphyrin group within the heme structure. 11 Follow-up work from the Princeton researchers demonstrated that the hemoglobin spectrum was polarization-dependent ( Figure 1) and confirmed Albrecht's vibronic theory of on-resonance Raman spectroscopy. 12 (Albrecht had theorized that onresonance Raman spectroscopy had different selection and polarization rules to off-resonance Raman spectroscopy.…”

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confidence: 53%

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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confidence: 53%

Raman Spectroscopy of Blood and Blood Components

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“…Resonance Raman spectra have recently been reported (11)(12)(13)(14)(15)(16)(17) for hemoglobin derivatives and for cytochrome c.…”

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Resonance Raman Spectra of Cobalt-Substituted Hemoglobin: Cooperativity and Displacement of the Cobalt Atom upon Oxygenation

Woodruff

Spiro

Yonetani

1974

Proc. Natl. Acad. Sci. U.S.A.

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The resonance Raman spectra of oxy and deoxy cobalt-substituted hemoglobin (CoHb) are reported. Comparison of these spectra to those of hemoglobin, methemoglobin, cytochrome c, and model cobalt porphyrin complexes suggests that the displacement of the cobalt atom upon oxygenation of CoHb is no greater than the out-of-plane distance in five-coordinate Co(II) porphyrins, 0.15 A. Combining this distance with the expected contraction of the cobalt-histidine bond, Ibers has estimated a maximum displacement of 0.37 A for the proximal histidine with respect to the heme plane upon oxygenation, about one-third the corresponding distance estimated for iron hemoglobin. The free energy of cooperativity for cobalt hemoglobin is also estimated to be onethird that of iron hemoglobin. These results are therefore consistent with Hopfield's distributed energy model, which predicts proportionality between proximal histidine displacement and the free energy of cooperativity. By implication they support Perutz's trigger mechanism for cooperativity.

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“…The resonance-enhanced Raman spectra of oxyand deoxyHb A, which exclusively arise from vibrational modes of the heme groups, have shown significant differences in the line positions and line intensities of the two hemoglobin derivatives [17,18]. It has been concluded that electronic properties of the heme iron as well as structural properties of the heme are reflected in the resonance Raman spectra and it has become possible to make tentative assigmennt of most of the observed Raman lines [18].…”

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confidence: 99%

“…Raman scattering studies were performed with an experimental set-up already described previously [17]. For excitation we used the 488-nm line (500mW) of an argon ion laser.…”

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confidence: 99%

Raman Study on the Two Quaternary States of Unligated Hemoglobin

Sussner¹,

Mayer²,

Brunner

et al. 1974

European Journal of Biochemistry

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To decide whether the change in the quaternary state of unligated hemoglobin affects the electronic and structural properties of the heme group unligated hemoglobins modified with bis-(N-maleimidomethy1)ether and 2,2'-dicarboxy-4,4'-diiodoacetamidoazobenzol, which are in the high-affinity form, have been compared with unligated normal deoxyhemoglobin A by absorption spectroscopy and Raman scattering. The absorption spectra show no difference in the frequency of the bands in the visible and near ultraviolet region but differences were found in peak height and shape of the Soret band. The Raman resonance spectra recorded between 300 and 1700 cm-l show no difference a t all. These spectral observations indicate that the change of the quaternary structure of unligated hemoglobin slightly influences the excited electronic states of the heme but does not alter the electronic ground state. Along with other spectroscopic evidence from Mossbauer and nuclear magnetic resonance spectroscopy this suggests that only a minor fraction of the free energy difference of ligand binding in the two quaternary states may originate from differences in the electronic properties of the heme in unligated hemoglobin.The cooperative function of hemoglobin and the structural alterations accompanying the ligation process have been rationalized in terms of the allosterical two-state model [l]. The two allosterical states of hemoglobin have been identified as the states which differ fundamentally in a number of structural and functional aspects, first of all in their quaternary structure and in their affinity towards 0, or CO [2-111.This has justified the concept that an all-or-none transition from one quaternary state to the other occurs a t a ligation degree which depends on the particular properties of the hemoglobin species and on the particular solution conditions. The two-state model may be considered as a suitable first-order description of hemoglobin function and therefore it may serve as a platform for the further investigation and discussion of hemoglobin properties.A question essential for an understanding of the molecular mechanisms involved in the hemoglobin function is where the free energy of interaction AF originates [12], i.e. whether it is localized a t a few specific sites [2] or distributed [13] over the protein structure in nonlocalizable smell portions. It has been proposed that the salt bridges [2] a t the interface of the subunits in deoxyhemoglobin which are Abbreviations. Hb, hemoglobin; NMR, nuclear magnetic resonance.disrupted upon oxygenation might be the location for a storage of a major fraction of the total of AF.Another site which suggests itself as a possible location for the storage of a t least a fraction of AF is the heme iron and the heme group. One can investigate this question by studying the electronic properties of the heme iron and structural details of the heme in the two quaternary states of hemoglobin both in the ligated and the unligated forms. This has been done recently by proton NMR studies of ...

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Resonance Raman scattering on the haem group of oxy- and deoxyhaemoglobin

Cited by 103 publications

References 9 publications

Raman Spectroscopy of Blood and Blood Components

Raman Spectroscopy of Blood and Blood Components

Resonance Raman Spectra of Cobalt-Substituted Hemoglobin: Cooperativity and Displacement of the Cobalt Atom upon Oxygenation

Raman Study on the Two Quaternary States of Unligated Hemoglobin

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