direkt zum Inhalt springen

direkt zum Hauptnavigationsmenü

Sie sind hier

TU Berlin

Inhalt des Dokuments

Suche

Suche nach Publikationen




alle Publikationen (Reviews, Articles, Meetings and Proceedings)

Conformational transitions and redox potential shifts of cytochrome P450 induced by immobilization
Zitatschlüssel ISI:000235135900013
Autor Todorovic, S and Jung, C and Hildebrandt, P and Murgida, D H
Seiten 119-127
Jahr 2006
ISSN 0949-8257
DOI 10.1007/s00775-005-0054-9
Adresse 233 SPRING STREET, NEW YORK, NY 10013 USA
Journal J. Biol. Inorg. Chem.
Jahrgang 11
Nummer 1
Monat JAN
Verlag SPRINGER
Zusammenfassung 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.
Typ der Publikation Article
Download Bibtex Eintrag

Zusatzinformationen / Extras

Direktzugang

Schnellnavigation zur Seite über Nummerneingabe

Diese Seite verwendet Matomo für anonymisierte Webanalysen. Mehr Informationen und Opt-Out-Möglichkeiten unter Datenschutz.