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TitleStructure-guided engineering of membrane-binding regions for surfactant-free solubilization of direct electron transfer-type alcohol dehydrogenase.
Journal, issue, pagesChem Commun (Camb), Vol. 62, Issue 31, Page 7948-7952, Year 2026
Publish dateApr 23, 2026
AuthorsKonatsu Ichikawa / Taiki Adachi / Tomoko Miyata / Fumiaki Makino / Keiichi Namba / Yuki Kitazumi / Osamu Shirai / Keisei Sowa /
PubMed AbstractMembrane-bound alcohol dehydrogenase (ADH) from is a direct electron transfer-type biocatalyst for ethanol oxidation. To improve its bioelectrocatalysis, membrane-binding regions of ADH were ...Membrane-bound alcohol dehydrogenase (ADH) from is a direct electron transfer-type biocatalyst for ethanol oxidation. To improve its bioelectrocatalysis, membrane-binding regions of ADH were predicted, resulting in the construction of a soluble ADH variant by enzyme engineering. The variant was purified and characterized using structural and bioelectrochemical approaches.
External linksChem Commun (Camb) / PubMed:41853871
MethodsEM (single particle)
Resolution2.69 - 2.71 Å
Structure data

66439

9x0q

EMDB-66439, PDB-9x0q:
Cryo-EM Structure of Alcohol Dehydrogenase Variant from Gluconobacter oxydans Truncating Membrane-Binding Regions (Form 1)
Method: EM (single particle) / Resolution: 2.71 Å

66440

9x0r

EMDB-66440, PDB-9x0r:
Cryo-EM Structure of Alcohol Dehydrogenase Variant from Gluconobacter oxydans Truncating Membrane-Binding Regions (Form 2)
Method: EM (single particle) / Resolution: 2.69 Å

Chemicals

ChemComp-HEC:
HEME C

ChemComp-PQQ:
PYRROLOQUINOLINE QUINONE

ChemComp-CA:
Unknown entry

Source
  • gluconobacter oxydans (bacteria)
KeywordsOXIDOREDUCTASE / Complex / Membrane-bound protein / Comples

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