Amino Acid Residues Controlling Domain Interaction and Interdomain Electron Transfer in Cellobiose Dehydrogenase.
cellobiose dehydrogenase
electron transfer
molecular dynamic simulation
multistate modeling
small angle X-ray scattering
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
16 Nov 2023
16 Nov 2023
Historique:
revised:
31
08
2023
received:
07
06
2023
pmc-release:
16
11
2024
medline:
20
11
2023
pubmed:
28
9
2023
entrez:
28
9
2023
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 37768852
doi: 10.1002/cbic.202300431
pmc: PMC10726044
mid: NIHMS1947086
doi:
Substances chimiques
cellobiose-quinone oxidoreductase
EC 1.1.99.18
Amino Acids
0
Fungal Proteins
0
Carbohydrate Dehydrogenases
EC 1.1.-
Mixed Function Oxygenases
EC 1.-
Polysaccharides
0
Cytochromes
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202300431Subventions
Organisme : NCI NIH HHS
ID : P01 CA092584
Pays : United States
Organisme : NIGMS NIH HHS
ID : P30 GM124169
Pays : United States
Organisme : NIGMS NIH HHS
ID : P30GM124169-01
Pays : United States
Informations de copyright
© 2023 The Authors. ChemBioChem published by Wiley-VCH GmbH.
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