Melanie Rupp's research while affiliated with University of Natural Resources and Life Sciences Vienna and other places

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Publications (1)

Models of the open state (4QI7, A) and the closed state (4QI6, B) of CDH. The FAD in the DH domain is shown in yellow, and the heme b in the CYT domain is red.
Ribbon structure of the interface between the DH and CYT domain in the closed state (4QI6) for the wild‐type MtCDH(A), M309A (B), R698S (C) and M309 A/R698S (D), showing the prosthetic groups (heme b, red; FAD, yellow, blue, orange) and the mutated side chains (M309, cyan; R698, blue) as sticks.
Production of wild‐type MtCDH (A), M309A (B), R698S (C), and M309A/R698S (D) in a 5 L bioreactor. The wet biomass (black circles), the protein concentration (purple triangles), and the activities determined using DCIP (cyan squares) or cytochrome c (green diamonds) as electron acceptor are shown.
FAD (A) and heme b (B) reduction kinetics of wild‐type MtCDH and variants at different pH values.
Pair‐distance‐distribution function of wild‐type MtCDH and all variants obtained at pH 3.5 (A), 5.5 (B), and 7.5 (C), calculated from the measured data shown in Figures S3–S7. (D) SAXS similarity plot to compare the individual curves (red: low similarity, blue: high similarity). The results from the 50 best‐fitting combinations, consisting of two models, were used to produce the histogram for pH 3.5 (E) and pH 7.5 (F).

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Amino Acid Residues Controlling Domain Interaction and Interdomain Electron Transfer in Cellobiose Dehydrogenase
  • Article
  • Full-text available

September 2023

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49 Reads

ChemBioChemChemBioChem

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Melanie Rupp

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The function of cellobiose dehydrogenase (CDH) in biosensors, biofuel cells, and as a physiological redox partner of lytic polysaccharide monooxygenase (LPMO) is based on its role as an electron donor. Before donating electrons to LPMO or electrodes, an interdomain electron transfer from the catalytic FAD‐containing dehydrogenase domain to the electron shuttling cytochrome domain of CDH is required. This study investigates the role of two crucial amino acids located at the dehydrogenase domain on domain interaction and interdomain electron transfer by structure‐based engineering. The electron transfer kinetics of wild‐type Myriococcum thermophilum CDH and its variants M309A, R698S, and M309A/R698S were analyzed by stopped‐flow spectrophotometry and structural effects were studied by small‐angle X‐ray scattering. The data show that R698 is essential to pull the cytochrome domain close to the dehydrogenase domain and orient the heme propionate group towards the FAD, while M309 is an integral part of the electron transfer pathway – its mutation reducing the interdomain electron transfer 10‐fold. Structural models and molecular dynamics simulations pinpoint the action of these two residues on the domain interaction and interdomain electron transfer.

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