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Journal article
Probing the versatility of cytochrome c by spectroscopic means: A Laudatio on resonance Raman spectroscopy
Journal of inorganic biochemistry, v 259, 112641
20 Jun 2024
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Abstract
Over the last 50 years resonance Raman spectroscopy has become an invaluable tool for the exploration of chromophores in biological macromolecules. Among them, heme proteins and metal complexes have attracted considerable attention. This interest results from the fact that resonance Raman spectroscopy probes the vibrational dynamics of these chromophores without direct interference from the surrounding. However, the indirect influence via through-bond and through-space chromophore-protein interactions can be conveniently probed and analyzed. This review article illustrates this point by focusing on class 1 cytochrome c, a comparatively simple heme protein generally known as electron carrier in mitochondria. The article demonstrates how through selective excitation of resonance Raman active modes information about the ligation, the redox state and the spin state of the heme iron can be obtained from band positions in the Raman spectra. The investigation of intensities and depolarization ratios emerged as tools for the analysis of in-plane and out-of-plane deformations of the heme macrocycle. The article further shows how resonance Raman spectroscopy was used to characterize partially unfolded states of oxidized cytochrome c. Finally, it describes its use for exploring structural changes due to the protein's binding to anionic surfaces like cardiolipin containing membranes.
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Details
- Title
- Probing the versatility of cytochrome c by spectroscopic means: A Laudatio on resonance Raman spectroscopy
- Creators
- Reinhard Schweitzer-Stenner (Corresponding Author) - Drexel University, Chemistry
- Publication Details
- Journal of inorganic biochemistry, v 259, 112641
- Publisher
- Elsevier
- Number of pages
- 30
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:001362105600001
- Scopus ID
- 2-s2.0-85196296649
- Other Identifier
- 991021885914904721
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Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Chemistry, Inorganic & Nuclear