ArticleProceedings of the National Academy of Sciences of the United States of America2012
Heme-protein vibrational couplings in cytochrome c provide a dynamic link that connects the heme-iron and the protein surface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
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- Hydroxo-bridged active site of flavodiiron NO reductase revealed by NRVS and DFT.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Disabling the Entatic Control of Methionine Ligation through Additive Destabilization of Ferric CytochromeInorganic chemistry · 2025Article
- Study of the Myosin Relay Helix Peptide by Molecular Dynamics Simulations, Pump-Probe and 2D Infrared Spectroscopy.International journal of molecular sciences · 2024Article
- Genetically Encoded Fluorescent Probe for Detection of Heme-Induced Conformational Changes in Cytochrome c.Biosensors · 2023Article
- Heme-Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case.Molecules (Basel, Switzerland) · 2022Review
- Exploring the folding energy landscapes of heme proteins using a hybrid AWSEM-heme model.Journal of biological physics · 2022Article
- The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c.Biochemistry · 2018Article
- Influence of heme c attachment on heme conformation and potential.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- What Can Be Learned from Nuclear Resonance Vibrational Spectroscopy: Vibrational Dynamics and Hemes.Chemical reviews · 2017Review
- Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c.Biochemistry · 2017Article
- Experimental and DFT Investigations Reveal the Influence of the Outer Coordination Sphere on the Vibrational Spectra of Nickel-Substituted Rubredoxin, a Model Hydrogenase Enzyme.Inorganic chemistry · 2017Article
- High-resolution monochromator for iron nuclear resonance vibrational spectroscopy of biological samples.Japanese journal of applied physics. Part 1, Regular papers & short notes · 2016Article
- Low frequency dynamics of the nitrogenase MoFe protein via femtosecond pump probe spectroscopy - Observation of a candidate promoting vibration.Journal of inorganic biochemistry · 2015Article
- Effects of protein structure on iron-polypeptide vibrational dynamic coupling in cytochrome c.Biochemistry · 2015Article
- On the possible role of protein vibrations in information processing in the brain: three Russian dolls.Frontiers in molecular neuroscience · 2015Article
- Investigations of heme distortion, low-frequency vibrational excitations, and electron transfer in cytochrome c.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Redox state dependence of axial ligand dynamics in Nitrosomonas europaea cytochrome c552.The journal of physical chemistry. B · 2013Article
- Investigations of the low-frequency spectral density of cytochrome c upon equilibrium unfolding.The journal of physical chemistry. B · 2013Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The active site of cytochrome c (Cyt c) consists of a heme covalently linked to a pentapeptide segment (Cys-X-X-Cys-His), which provides a link between the heme and the protein surface, where the redox partners of Cyt c bind. To elucidate the vibrational properties of heme c, nuclear resonance vibrational spectroscopy (NRVS) measurements were performed on (57)Fe-labeled ferric Hydrogenobacter thermophilus cytochrome c(552), including (13)C(8)-heme-, (13)C(5)(15)N-Met-, and (13)C(15)N-polypeptide (pp)-labeled samples, revealing heme-based vibrational modes in the 200- to 450-cm(-1) spectral region. Simulations of the NRVS spectra of H. thermophilus cytochrome c(552) allowed for a complete assignment of the Fe vibrational spectrum of the protein-bound heme, as well as the quantitative determination of the amount of mixing between local heme vibrations and pp modes from the Cys-X-X-Cys-His motif. These results provide the basis to propose that heme-pp vibrational dynamic couplings play a role in electron transfer (ET) by coupling vibrations of the heme directly to vibrations of the pp at the protein-protein interface. This could allow for the direct transduction of the thermal (vibrational) energy from the protein surface to the heme that is released on protein/protein complex formation, or it could modulate the heme vibrations in the protein/protein complex to minimize reorganization energy. Both mechanisms lower energy barriers for ET. Notably, the conformation of the distal Met side chain is fine-tuned in the protein to localize heme-pp mixed vibrations within the 250- to 400-cm(-1) spectral region. These findings point to a particular orientation of the distal Met that maximizes ET.
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