Dokument-ID Dokumenttyp Verfasser/Autoren Herausgeber Haupttitel Abstract Auflage Verlagsort Verlag Erscheinungsjahr Seitenzahl Schriftenreihe Titel Schriftenreihe Bandzahl ISBN Quelle der Hochschulschrift Konferenzname Quelle:Titel Quelle:Jahrgang Quelle:Heftnummer Quelle:Erste Seite Quelle:Letzte Seite URN DOI Abteilungen OPUS4-55148 Wissenschaftlicher Artikel Neumann, Bettina; Kielb, Patrycja; Rustam, Lina; Fischer, Anna; Weidinger, Inez M.; Wollenberger, Ulla Bioelectrocatalytic Reduction of Hydrogen Peroxide by Microperoxidase-11 Immobilized on Mesoporous Antimony-Doped Tin Oxide The heme-undecapeptide microperoxidase-11 (MP-11) was immobilized on mesoporous antimony-doped tin oxide (ATO) thin-film electrodes modified with the positively charged binding promotor polydiallyldimethylammonium chloride. Surface concentrations of MP-11 of 1.5 nmol cm(-2) were sufficiently high to enable spectroelectrochemical analyses. UV/Vis spectroscopy and resonance Raman spectroscopy revealed that immobilized MP-11 adopts a six-coordinated low-spin conformation, as in solution in the presence of a polycation. Cathodic reduction of hydrogen peroxide at potentials close to +500mV versus Ag/AgCl indicates that the reaction proceeds via a Compound I-type like intermediate, analogous to natural peroxidases, and confirms mesoporous ATO as a suitable host material for adsorbing the heme-peptide in its native state. A hydrogen peroxide sensor is proposed by using the bioelectrocatalytic properties of the MP-11-modified ATO. Weinheim Wiley-VCH 2017 7 ChemElectrChem 4 4 913 919 10.1002/celc.201600776 Institut für Biochemie und Biologie OPUS4-38818 Wissenschaftlicher Artikel Kielb, Patrycja; Sezer, Murat; Katz, Sagie; Lopez, Francesca; Schulz, Christopher; Gorton, Lo; Ludwig, Roland; Wollenberger, Ursula; Zebger, Ingo; Weidinger, Inez M. Spectroscopic Observation of Calcium-Induced Reorientation of Cellobiose Dehydrogenase Immobilized on Electrodes and its Effect on Electrocatalytic Activity Cellobiose dehydrogenase catalyzes the oxidation of various carbohydrates and is considered as a possible anode catalyst in biofuel cells. It has been shown that the catalytic performance of this enzyme immobilized on electrodes can be increased by presence of calcium ions. To get insight into the Ca2+-induced changes in the immobilized enzyme we employ surface-enhanced vibrational (SERR and SEIRA) spectroscopy together with electrochemistry. Upon addition of Ca2+ ions electrochemical measurements show a shift of the catalytic turnover signal to more negative potentials while SERR measurements reveal an offset between the potential of heme reduction and catalytic current. Comparing SERR and SEIRA data we propose that binding of Ca2+ to the heme induces protein reorientation in a way that the electron transfer pathway of the catalytic FAD center to the electrode can bypass the heme cofactor, resulting in catalytic activity at more negative potentials. Weinheim Wiley-VCH 2015 9 ChemPhysChem : a European journal of chemical physics and physical chemistry 16 9 1960 1968 10.1002/cphc.201500112 Institut für Biochemie und Biologie OPUS4-37962 Wissenschaftlicher Artikel Albrecht, Steve; Vandewal, Koen; Tumbleston, John R.; Fischer, Florian S. U.; Douglas, Jessica D.; Frechet, Jean M. J.; Ludwigs, Sabine; Ade, Harald W.; Salleo, Alberto; Neher, Dieter On the efficiency of charge transfer state splitting in polymer: Fullerene solar cells Weinheim Wiley-VCH 2014 7 Advanced materials 26 16 2533 2539 10.1002/adma.201305283 Institut für Physik und Astronomie