ArticleProceedings of the National Academy of Sciences of the United States of America2014
Investigations of heme distortion, low-frequency vibrational excitations, and electron transfer in cytochrome c.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Methionine coordination to the heme iron and its displacement by nitric oxide in the CcoP subunit of Pseudomonas aeruginosa cytochrome cbbJournal of inorganic biochemistry · 2026Article
- Mechanisms of heme transport in the mitochondria.Biochemical Society transactions · 2025Review
- The flexible chain: regulation of structure and activity of ETC complexes defines rate of ATP synthesis and sites of superoxide generation.Biophysical reviews · 2025Review
- The H-NOX protein structure adapts to different mechanisms in sensors interacting with nitric oxide.Chemical science · 2023Article
- Reactivity Factors in Catalytic Methanogenesis and Their Tuning upon Coenzyme F430 Biosynthesis.Journal of the American Chemical Society · 2023Article
- Prediction of Protein Function from Tertiary Structure of the Active Site in Heme Proteins by Convolutional Neural Network.Biomolecules · 2023Article
- Absolute excited state molecular geometries revealed by resonance Raman signals.Nature communications · 2022Article
- Elucidation of the Correlation between Heme Distortion and Tertiary Structure of the Heme-Binding Pocket Using a Convolutional Neural Network.Biomolecules · 2022Article
- A 300-fold conductivity increase in microbial cytochrome nanowires due to temperature-induced restructuring of hydrogen bonding networks.Science advances · 2022Article
- Multiple Mutations in the Non-Ordered Red Ω-Loop Enhance the Membrane-Permeabilizing and Peroxidase-like Activity of CytochromeBiomolecules · 2022Article
- Analysis of Fluctuation in the Heme-Binding Pocket and Heme Distortion in Hemoglobin and Myoglobin.Life (Basel, Switzerland) · 2022Article
- Excited-State Energy Surfaces in Molecules Revealed by Impulsive Stimulated Raman Excitation Profiles.The journal of physical chemistry letters · 2021Article
- PyDISH: database and analysis tools for heme porphyrin distortion in heme proteins.Database : the journal of biological databases and curation · 2020Article
- Spin cascade and doming in ferric hemes: Femtosecond X-ray absorption and X-ray emission studies.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Ultrafast Dynamics and Vibrational Relaxation in Six-Coordinate Heme Proteins Revealed by Femtosecond Stimulated Raman Spectroscopy.Journal of the American Chemical Society · 2020Article
- Spectral Characterization of a Novel NO Sensing Protein in Bacteria: NosP.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
- Article
- Challenging Density Functional Theory Calculations with Hemes and Porphyrins.International journal of molecular sciences · 2016Review
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Authors and funding
6 authors.
Funding
Abstract
Cytochrome (cyt) c is an important electron transfer protein. The ruffling deformation of its heme cofactor has been suggested to relate to its electron transfer rate. However, there is no direct experimental evidence demonstrating this correlation. In this work, we studied Pseudomonas aeruginosa cytochrome c551 and its F7A mutant. These two proteins, although similar in their X-ray crystal structure, display a significant difference in their heme out-of-plane deformations, mainly along the ruffling coordinate. Resonance Raman and vibrational coherence measurements also indicate significant differences in ruffling-sensitive modes, particularly the low-frequency γa mode found between ∼50-60 cm(-1). This supports previous assignments of γa as having a large ruffling content. Measurement of the photoreduction kinetics finds an order of magnitude decrease of the photoreduction cross-section in the F7A mutant, which has nearly twice the ruffling deformation as the WT. Additional measurements on cytochrome c demonstrate that heme ruffling is correlated exponentially with the electron transfer rates and suggest that ruffling could play an important role in redox control. A major relaxation of heme ruffling in cytochrome c, upon binding to the mitochondrial membrane, is discussed in this context.
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