Structural investigation of cellobiose dehydrogenase IIA: Insights from small angle scattering into intra- and intermolecular electron transfer mechanisms.

摘要: Abstract Background Cellobiose dehydrogenases have gained interest due to their potential applications in sectors from biofuel production biomedical devices. The CDHIIA variant is comprised of a cytochrome domain (CYT), dehydrogenase (DH), and carbohydrate-binding module (CBM) that are connected by two flexible linkers. Upon cellobiose oxidation at the DH, intramolecular electron transfer (IaET) occurs DH CYT. In vivo, CYT subsequently performs intermolecular (IeET) lytic polysaccharide monooxygenase (LPMO). relevant solution-state CDH conformations for IaET IeET not been fully characterized. Methods Small-angle X-ray neutron scattering measurements oxidized Myriococcum thermophilum Neurospora crassa were performed investigate structural landscape explored solution MtCDHIIA NcCDHIIA response cations, pH, presence an acceptor, LPMO9D N. crassa. Results data complemented modeling show that, under oxidizing conditions, undergoes global conformational rearrangement Ca2+. Oxidized exhibits changes upon pH variation and, NcLPMO9D, primarily adopts compact conformation. Conclusions These results demonstrate different responses environment. also reveal shift toward interdomain compaction co-incubation with NcLPMO9D. General significance present study first report on landscapes various cation concentrations, conditions electron-accepting LPMO.