ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2006
Conformational transitions and redox potential shifts of cytochrome P450 induced by immobilization.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Phosphorylation of cytochrome c at tyrosine 48 finely regulates its binding to the histone chaperone SET/TAF-Iβ in the nucleus.Protein science : a publication of the Protein Society · 2024Article
- Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases.BBA advances · 2024Article
- How to Turn an Electron Transfer Protein into a Redox Enzyme for Biosensing.Molecules (Basel, Switzerland) · 2021Review
- SERR Spectroelectrochemistry as a Guide for Rational Design of DyP-Based Bioelectronics Devices.International journal of molecular sciences · 2021Article
- Resonance Raman view of the active site architecture in bacterial DyP-type peroxidases.RSC advances · 2020Review
- Nanoscale electron transport measurements of immobilized cytochrome P450 proteins.Nanotechnology · 2015Article
- Article
- Electrochemistry of mammalian cytochrome P450 2B4 indicates tunable thermodynamic parameters in surfactant films.Journal of inorganic biochemistry · 2013Article
- Measurement of electron transfer through cytochrome P450 protein on nanopillars and the effect of bound substrates.Journal of the American Chemical Society · 2013Article
- Bioelectronic delivery of electrons to cytochrome P450 enzymes.The journal of physical chemistry. B · 2011Article
- Substrate binding to cytochromes P450.Analytical and bioanalytical chemistry · 2008Review
- Active-site structure, binding and redox activity of the heme-thiolate enzyme CYP2D6 immobilized on coated Ag electrodes: a surface-enhanced resonance Raman scattering study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2008Article
- XH/pi interactions with the pi system of porphyrin ring in porphyrin-containing proteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2007Article
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4 authors.
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Abstract
Cytochrome P450 (P450) from Pseudomonas putida was immobilized on Ag electrodes coated with self-assembled monolayers (SAMs) via electrostatic and hydrophobic interactions as well as by covalent cross-linking. The redox and conformational equilibria of the immobilized protein were studied by potential-dependent surface-enhanced resonance Raman spectroscopy. All immobilization conditions lead to the formation of the cytochrome P420 (P420) form of the enzyme. The redox potential of the electrostatically adsorbed P420 is significantly more positive than in solution and shows a steady downshift upon shortening of the length of the carboxyl-terminated SAMs, i.e., upon increasing the strength of the local electric field. Thus, two opposing effects modulate the redox potential of the adsorbed enzyme. First, the increased hydrophobicity of the heme environment brought about by immobilization on the SAM tends to upshift the redox potential by stabilizing the formally neutral ferrous form. Second, increasing electric fields tend to stabilize the positively charged ferric form, producing the opposite effect. The results provide insight into the parameters that control the structure and redox properties of heme proteins and contribute to the understanding of the apparently anomalous behavior of P450 enzymes in bioelectronic devices.
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