Resonance Raman spectra of octaethylporphyrinato-Ni(II) and m
 e
 s
 o-deuterated and 15N substituted derivatives. I. Observation and assignments of nonfundamental Raman lines

Kitagawa, Teizo; Abe, Mitsutomo; Ogoshi, Hisanobu

doi:10.1063/1.436441

Cited by 157 publications

(90 citation statements)

References 43 publications

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“…We may conclude that any movement of the heme iron from the plane of the pyrrole nitrogen atoms, associated with the R-T transition in deoxyhemoglobin, is not caused by alterations in the core size. In a recent normal coordinate analysis the 674 cm-1 line was shown to be a breathing mode of the 16-membered macrocycle (17,18) and thereby to have considerable pyrrole nitrogen-to-Fe stretching character.s In addition, in model Fe(II) complexes this metal-sensitive line changes frequency when the axial ligand is varied (19), but the frequency change does not correlate with the extent of back donation. We can place a limit on the frequency difference of this line between the R and T quaternary structures of less than 0.1 cm-'.…”

Section: Resultsmentioning

confidence: 99%

Protein-heme interaction in hemoglobin: evidence from Raman difference spectroscopy.

Shelnutt¹,

Rousseau²,

Friedman³

et al. 1979

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

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Raman difference spectroscopy measurements on native and chemically modified human deoxyhemoglobins stabilized in either the R or the T quaternary structure revealed frequency differences in the oxidation state marker lines. The differences indicate that the R structure has an effective increase in the electron density of the antibonding 7r* orbitals of the porphyrin rings. This increase is explained by a charge transfer interaction between donor orbitals and the lr* orbitals of the porphyrins. The relative amount of charge transferred, which is inferred from the Raman difference measurements, correlates with some but not all factors that influence the energetics of toe quaternary structure equilibrium. In addition, the free energy of cooperativity for a variety of ligated proteins follows the same order as that of the degree of charge depletion of the r* orbitals upon ligation as determined from the frequency of a Raman mode. The proposed electronic interaction between the protein and heme could result in energies large enough to provide a significant contribution to the energetics of hemoglobin cooperativity.The understanding of the molecular basis for cooperativity in the oxygenation of hemoglobin depends on being able to identify the origin of the difference, AG, in free energy of ligand binding between the low-affinity (T) and high-affinity (R) quaternary structures (1, 2). AG has been proposed by some to be lqalized at the heme (3) and by others to be distributed throughout the protein (4-6). We find evidence for a protein-heme interaction and we conclude that there is a contribution to AG, the free energy of cooperativity, which is detected at the porphyrin. This evidence, derived from Raman difference spectroscopy (RDS), suggests that AG contains an electronic stabilization energy resulting from a charge transfer interaction.Pue to resonance enhancement, the heme protein Raman spectra obtained with visible excitation frequencies contain only those vibrational modes associated with the porphyrin macrocycle. Consequently protein influences on the properties of the prirphyrin ring may be studied by comparing the resonance Raman spectrum of molecules in which there are differences in the structure of the protein. In previous resonance Raman scattering studies of deoxyhemoglobins (7-11), which have attempted to locate bond strain and test cooperativity models, no differences in the Raman frequencies between the two quaternary structures were found. However, the lower limit for the detection of reliable frequency differences in hemoglobin has been about 1-2 cm-l. Recently Shelnutt et al. (12) reported on a RDS technique in which they reliably detected frequency differences as small as 0.1 cm-l in cytochromes c by simultaneously acquiring the Raman spectrum of two samples and by subsequent data processing on a minicomputer. We have now used this technique to compare native deoxyhemoglobin in the T structure and chemically modified deoxyhemoglobins stabilized in either the R or T structures. MATERIALS A...

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Section: Resultsmentioning

confidence: 99%

Protein-heme interaction in hemoglobin: evidence from Raman difference spectroscopy.

Shelnutt¹,

Rousseau²,

Friedman³

et al. 1979

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

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“…Detailed analysis of resonance Raman spectra of metallo porphyrins have been worked out with Ni(II)-octaethylporphyrin, Ni(OEP), and its isotope derivatives, 66,67 and the vibrational assignments were later improved 68 -70 and extended to proteins such as cytochrome c (cyt c) 71 and Mb. 72 The visRR spectra in the high frequency region (1200-1700 cm 1 ), where skeletal stretching vibrations of porphyrin macrocycle appear, reflect the oxidation state, coordination number, and the spin state of the heme iron.…”

Section: Heme Skeletal Vibrational Modesmentioning

confidence: 99%

Raman Spectroscopy of Proteins

Kitagawa¹,

Hirota²

2001

Handbook of Vibrational Spectroscopy

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The sections in this article are Introduction General Aspects of Ordinary R aman Spectra of Proteins Amides I and III Frequencies and Secondary Structures T rp Bands and Microenvironments of T rp Residues T yr Bands and Hydrogen Bonding Histidine Band and Protonation S  S Stretching Frequency and Conformation of Disulfide Bridge UV Resonance R aman Spectra of Proteins Amide Modes Tyrosine‐Related Modes Tryptophan‐Related Modes Histidine‐Related Modes Cysteine‐Related Modes X ‐Proline Vibrational Modes Modes of Metal‐Coordinated Residues Visible Resonance R aman Spectra of Proteins Heme Proteins Heme Skeletal Vibrational Modes Fe  H is and Fe  C ys stretching modes Fe ( II )‐ O 2 Related Modes Fe ( II )‐ CO Related Modes Fe ( III )‐ CN Related Modes Fe ( II )‐ NO and Fe ( III )‐ NO Related Modes Fe ( III )‐ OH Related Modes Fe ( IV ) O Related Modes Copper Proteins Quinone Vibrations of Quinoproteins Tyrosine Radical Modes in Proteins Flavo Proteins Vis RR Spectra of Other Proteins

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“…Most of the Raman and IR bands appear to occur at approximately the same position ( < 20 cm-l ) as those observed for NiOEP [6][7][8]. Therefore, we use the NiOEP data [6][7][8][9][10] for band assignment. Table 1 collects the assignments of the Raman bands.…”

Section: Raman Spectroscopymentioning

confidence: 99%

An in-situ Raman study of the effect of the support for adsorbed iridium-chelates in catalysing oxygen reduction

Bouwkamp-Wijnoltz

Pałys

Visscher

et al. 1996

Journal of Electroanalytical Chemistry

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Resonance Raman spectra of octaethylporphyrinato-Ni(II) and m e s o-deuterated and 15N substituted derivatives. I. Observation and assignments of nonfundamental Raman lines

Cited by 157 publications

References 43 publications

Protein-heme interaction in hemoglobin: evidence from Raman difference spectroscopy.

Protein-heme interaction in hemoglobin: evidence from Raman difference spectroscopy.

Raman Spectroscopy of Proteins

An in-situ Raman study of the effect of the support for adsorbed iridium-chelates in catalysing oxygen reduction

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