Polarized resonance Raman dispersion spectroscopy on metalporphyrins

Schweitzer‐Stenner, Reinhard

doi:10.1002/jpp.307

Cited by 25 publications

(99 citation statements)

References 65 publications

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“…If this was the case, the band would be practically undetectable in the entire preresonance and resonance regions of the Q-band, contrary to what the excitation profile in Figure 5 suggests. In reality, the ] 4 -band gains considerable Raman activity from Herzberg-Teller coupling [19,60,62,63].…”

Section: Asymmetric Deformations Of the Functional Heme Groupmentioning

confidence: 99%

“…The underlying theory utilized to analyze the data in Figure 5 is rather complex and has been described in several papers and comprehensive review articles [11,19]. Since this paper focuses on structural and related functional properties of cytochrome c, we consider only the structural information that emerged from the analysis of the Raman data.…”

Section: Asymmetric Deformations Of the Functional Heme Groupmentioning

confidence: 99%

“…This implies that a perturbation potential has to be added tôthat is produced by the peripheral substituents and the protein environment [19,66]:…”

Section: Asymmetric Deformations Of the Functional Heme Groupmentioning

confidence: 99%

“…Figure 5) in the region between the 0 and the V resonances. However, the contribution of antisymmetric vibronic coupling is negligible outside of the -band region [19,43]. Thus the dispersion between -and -band region must result from 1 -and 2 -type deformations.…”

Section: Asymmetric Deformations Of the Functional Heme Groupmentioning

confidence: 99%

“…The protein has also been utilized as a model system for protein folding studies [18]. The research in our laboratories has mostly been focused on elucidating heme-protein interactions and asymmetric deformations of the heme macrocycle [11,19], but lately we used spectroscopic means to probe partially unfolded states of the protein [20]. The second chapter of this review describes how heme-protein interactions affecting the prosthetic heme group of cytochrome can be probed by resonance Raman, visible circular dichroism, and low temperature absorption spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

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Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility

Schweitzer‐Stenner

2014

New Journal of Science

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Cytochrome has served as a model system for studying redox reactions, protein folding, and more recently peroxidase activity induced by partial unfolding on membranes. This review illuminates some important aspects of the research on this biomolecule. The first part summarizes the results of structural analyses of its active site. Owing to heme-protein interactions the heme group is subject to both in-plane and out-of-plane deformations. The unfolding of the protein as discussed in detail in the second part of this review can be induced by changes of pH and temperature and most prominently by the addition of denaturing agents. Both the kinetic and thermodynamic folding and unfolding involve intermediate states with regard to all unfolding conditions. If allowed to sit at alkaline pH (11.5) for a week, the protein does not return to its folding state when the solvent is switched back to neutral pH. It rather adopts a misfolded state that is prone to aggregation via domain swapping. On the surface of cardiolipin containing liposomes, the protein can adopt a variety of partially unfolded states. Apparently, ferricytochrome c can perform biological functions even if it is only partially folded.

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Section: Asymmetric Deformations Of the Functional Heme Groupmentioning

confidence: 99%

Section: Asymmetric Deformations Of the Functional Heme Groupmentioning

confidence: 99%

“…This implies that a perturbation potential has to be added tôthat is produced by the peripheral substituents and the protein environment [19,66]:…”

Section: Asymmetric Deformations Of the Functional Heme Groupmentioning

confidence: 99%

Section: Asymmetric Deformations Of the Functional Heme Groupmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility

Schweitzer‐Stenner

2014

New Journal of Science

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Non‐planar heme deformations and excited state displacements in horseradish peroxidase detected by Raman spectroscopy at Soret excitation

Huang

Schweitzer‐Stenner

2005

J Raman Spectroscopy

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We studied the out-of-plane modes of horseradish peroxidase (HRP) in different spin, oxidation and ligation states by measuring the respective resonance Raman spectra with (near) Soret excitation. The non-planar modes of the heme are Raman inactive for planar macrocycles, but become resonance Raman active in the presence of out-of-plane deformations. The thus induced Raman scattering results mostly from Franck-Condon type coupling. We observed bands from a variety of out-of-plane modes such as g 5 , g 6 , g 7 .A 2u / modes, g 21 and g 22 .E g /, g 15 .B 2u / and g 11 .B 1u /. The appearance of these bands is clearly indicative of non-planar deformations of the same symmetry. We determined the relative intensities of all sufficiently intense Raman modes of ferric pentacoordinated, quantum mixed and hexacoordinated low-spin as well as of ferrous pentacoordinated high-spin HRP C. The apparent vibronic coupling parameters were obtained from a self-consistent analysis of the Raman intensities and the respective optical absorption spectrum. They revealed significantly reduced displacements of the excited B-state for the ferrous, deoxy-like state compared with the resting ferric state. An analysis of the obtained coupling strengths of out-of-plane modes revealed that they are predominantly induced by static non-planar deformations along the normal coordinates of the lowest wavenumber modes of a given symmetry type. We used the deformations of the heme in resting HRP C to determine the vibronic coupling strength of the experimentally detectable out-of-plane modes and subsequently employed this information to obtain the non-planar deformations for the investigated ferric hexacoordinated low-spin state. This yielded a substantial reduction of the ruffling distortion, whereas the doming deformation remained mostly unaffected by the change of the iron's spin and ligation state.

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Out‐of‐plane deformations of the heme group in different ferrocytochrome c proteins probed by resonance Raman spectroscopy

Hagarman

Wallace

Laberge

et al. 2008

J Raman Spectroscopy

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We measured the low-wavenumber polarized resonance Raman spectra of horse heart (hhc), chicken (chc) and yeastC102T (yc) ferrocytochromes c with Soret excitation. We examined the out-of-plane (oop) deformations of the heme groups by virtue of relative intensities and depolarization ratios of a variety of oop and in-plane (ip) Raman active bands. Analysis of relative Raman intensities shows differences in deviation from planarity of the heme groups of yeast, horse heart and chicken cytochromes c. The heme groups in cytochrome c proteins have been shown by normal coordinate static deformation (NSD) analysis from crystal structures to exhibit a dominant ruffling (B 1u ) deformation. As a consequence the B 1u modes, g 10 − g 12 , become resonance Raman active. We used normalized Raman intensity ratios and depolarization ratios of oop Raman active modes, whose intensities are attributable to specific nonplanar deformations, to estimate and compare their Franck-Condon-type and Jahn-Teller-type coupling magnitudes for horse heart, chicken and yeast ferrocytochrome c at neutral pH. These coupling magnitudes allow for a quantitative comparison of oop deformations between individual heme groups. Chicken ferrocytochrome was found to have the largest ruffling deformation of the three investigated proteins, followed by horse heart and yeast cytochrome c. The heme group of the former is slightly more ruffled than the corresponding active site of the latter, while saddling in both proteins is substantially larger than in chicken ferrocytochrome c. The Raman data are sensitive enough to allow a comparison of lesser deformations. Doming, which is a kinetic coordinate in many heme proteins, is largest in chicken and smallest in yeast cytochrome c. Waving is largest in yeast, followed by horse heart and chicken cytochrome c. Propellering deformations could be compared for chicken and horse heart cytochrome c and were found to be substantially larger in the latter. A comparison with heme deformations obtained from X-ray structures (for horse heart and yeast cytochrome c) and from molecular dynamics simulations (MDS) (performed for all three proteins) yields some agreement with the main ruffling and saddling deformations derived from the crystal structures, whereas the heme conformations produced by MDS seem to account better for smaller deformations like doming and propellering. The present study demonstrates the usefulness of resonance Raman spectroscopy for the analysis of nonplanar deformations in heme proteins.

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Polarized resonance Raman dispersion spectroscopy on metalporphyrins

Cited by 25 publications

References 65 publications

Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility

Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility

Non‐planar heme deformations and excited state displacements in horseradish peroxidase detected by Raman spectroscopy at Soret excitation

Out‐of‐plane deformations of the heme group in different ferrocytochrome c proteins probed by resonance Raman spectroscopy

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