ArticleInorganic chemistry2011
Modulation of ligand-field parameters by heme ruffling in cytochromes c revealed by EPR spectroscopy.
Article in Inorganic chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Heme-Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case.Molecules (Basel, Switzerland) · 2022Review
- Molecular mechanisms of electron transfer employed by native proteins and biological-inorganic hybrid systems.Computational and structural biotechnology journal · 2021Review
- 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
- 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
- Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferrihemeChemical science · 2016Article
- Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Biochimica et biophysica acta · 2016Review
- Effects of protein structure on iron-polypeptide vibrational dynamic coupling in cytochrome c.Biochemistry · 2015Article
- The structure of ferricytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H.Metallomics : integrated biometal science · 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
- The influence of heme ruffling on spin densities in ferricytochromes c probed by heme core 13C NMR.Inorganic chemistry · 2013Article
- Structural characterization of nitrosomonas europaea cytochrome c-552 variants with marked differences in electronic structure.Chembiochem : a European journal of chemical biology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Electron paramagnetic resonance (EPR) spectra of variants of Hydrogenobacter thermophilus cytochrome c(552) (Ht c-552) and Pseudomonas aeruginosa cytochrome c(551) (Pa c-551) are analyzed to determine the effect of heme ruffling on ligand-field parameters. Mutations introduced at positions 13 and 22 in Ht c-552 were previously demonstrated to influence hydrogen bonding in the proximal heme pocket and to tune reduction potential (E(m)) over a range of 80 mV [Michel, L. V.; Ye, T.; Bowman, S. E. J.; Levin, B. D.; Hahn, M. A.; Russell, B. S.; Elliott, S. J.; Bren, K. L. Biochemistry 2007, 46, 11753-11760]. These mutations are shown here to also increase heme ruffling as E(m) decreases. The primary effect on electronic structure of increasing heme ruffling is found to be a decrease in the axial ligand-field term Δ/λ, which is proposed to arise from an increase in the energy of the d(xy) orbital. Mutations at position 7, previously demonstrated to influence heme ruffling in Pa c-551 and Ht c-552, are utilized to test this correlation between molecular and electronic structure. In conclusion, the structure of the proximal heme pocket of cytochromes c is shown to play a role in determining heme conformation and electronic structure.
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