TY  - JOUR
A1  - Rübsam, Kristin
A1  - Stomps, Benjamin René Harald
A1  - Böker, Alexander
A1  - Jakob, Felix
A1  - Schwaneberg, Ulrich
T1  - Anchor peptides: A green and versatile method for polypropylene functionalization
JF  - Polymer : the international journal for the science and technology of polymers
KW  - Material binding peptides
KW  - Anchor peptides
KW  - Surface modification
KW  - Immobilization
Y1  - 2017
U6  - https://doi.org/10.1016/j.polymer.2017.03.070
SN  - 0032-3861
SN  - 1873-2291
VL  - 116
SP  - 124
EP  - 132
PB  - Elsevier
CY  - Oxford
ER  - 
TY  - JOUR
A1  - Spricigo, Roberto
A1  - Leimkühler, Silke
A1  - Gorton, Lo
A1  - Scheller, Frieder W.
A1  - Wollenberger, Ursula
T1  - The Electrically Wired Molybdenum Domain of Human Sulfite Oxidase is Bioelectrocatalytically Active
JF  - European journal of inorganic chemistry : a journal of ChemPubSoc Europe
N2  - We report electron transfer between the catalytic molybdenum cofactor (Moco) domain of human sulfite oxidase (hSO) and electrodes through a poly(vinylpyridine)-bound [osmium(N,N'-methyl-2,2'-biimidazole)(3)](2+/3+) complex as the electron-transfer mediator. The biocatalyst was immobilized in this low-potential redox polymer on a carbon electrode. Upon the addition of sulfite to the immobilized separate Moco domain, the generation of a significant catalytic current demonstrated that the catalytic center is effectively wired and active. The bioelectrocatalytic current of the wired separate catalytic domain reached 25% of the signal of the wired full molybdoheme enzyme hSO, in which the heme b(5) is involved in the electron-transfer pathway. This is the first report on a catalytically active wired molybdenum cofactor domain. The formal potential of this electrochemical mediator is between the potentials of the two cofactors of hSO, and as hSO can occupy several conformations in the polymer matrix, it is imaginable that electron transfer from the catalytic site to the electrode through the osmium center occurs for the hSO molecules in which the Moco domain is sufficiently accessible. The observation of catalytic oxidation currents at low potentials is favorable for applications in bioelectronic devices.
KW  - Metalloenzymes
KW  - Enzyme catalysis
KW  - Immobilization
KW  - Osmium
Y1  - 2015
U6  - https://doi.org/10.1002/ejic.201500034
SN  - 1434-1948
SN  - 1099-0682
IS  - 21
SP  - 3526
EP  - 3531
PB  - Wiley-VCH
CY  - Weinheim
ER  - 
TY  - JOUR
A1  - Sarauli, David
A1  - Xu, Chenggang
A1  - Dietzel, Birgit
A1  - Schulz, Burkhard
A1  - Lisdat, Fred
T1  - Differently substituted sulfonated polyanilines - the role of polymer compositions in electron transfer with pyrroloquinoline quinone-dependent glucose dehydrogenase
JF  - Acta biomaterialia
N2  - Sulfonated polyanilines have become promising building blocks in the construction of biosensors, and therefore we use here differently substituted polymer forms to investigate the role of their structural composition and properties in achieving a direct electron transfer with the redox enzyme pyrroloquinoline quinone-dependent glucose dehydrogenase (PQQ-GDH). To this end, new copolymers containing different ratios of 2-methoxyaniline-5-sulfonic acid (MAS), 3-aminobenzenesulfonic acid (ABS) and 3-aminobenzoic acid (AB) units have been chemically synthesized. All polymers have been studied with respect to their ability to react directly with PQQ-GDH. This interaction has been monitored initially in solution, and subsequently on electrode surfaces. The results show that only copolymers with MAS and aniline units can directly react with PQQ-GDH in solution; the background can be mainly ascribed to the emeraldine salt redox state of the polymer, allowing rather easy reduction. However, when polymers and the enzyme are immobilized on the surface of carbon nanotube-containing electrodes, direct bioelectrocatalysis is also feasible in the case of copolymers composed of ABS/AB and MAS/AB units, existing initially in pernigraniline base form. This verifies that a productive interaction of the enzyme with differently substituted polymers is feasible when the electrode potential can be used to drive the reaction towards the oxidation of the substrate-reduced enzyme. These results clearly demonstrate that enzyme electrodes based on sulfonated polyanilines and direct bioelectrocatalysis can be successfully constructed.
KW  - Sulfonated polyaniline
KW  - PQQ-dependent glucose dehydrogenase
KW  - Direct electron transfer
KW  - Immobilization
KW  - Bioelectrocatalysis
Y1  - 2013
U6  - https://doi.org/10.1016/j.actbio.2013.06.008
SN  - 1742-7061
VL  - 9
IS  - 9
SP  - 8290
EP  - 8298
PB  - Elsevier
CY  - Oxford
ER  -