Structure at 1.9 A Resolution of a Quinohemoprotein Alcohol Dehydrogenase From Pseudomonas Putida HK5

Structure. 2002 Jun;10(6):837-49. doi: 10.1016/s0969-2126(02)00774-8.


The type II quinohemoprotein alcohol dehydrogenase of Pseudomonas putida is a periplasmic enzyme that oxidizes substrate alcohols to the aldehyde and transfers electrons first to pyrroloquinoline quinone (PQQ) and then to an internal heme group. The 1.9 A resolution crystal structure reveals that the enzyme contains a large N-terminal eight-stranded beta propeller domain (approximately 60 kDa) similar to methanol dehydrogenase and a small C-terminal c-type cytochrome domain (approximately 10 kDa) similar to the cytochrome subunit of p-cresol methylhydoxylase. The PQQ is bound near the axis of the propeller domain about 14 A from the heme. A molecule of acetone, the product of the oxidation of isopropanol present during crystallization, appears to be bound in the active site cavity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alcohol Oxidoreductases / chemistry*
  • Alcohol Oxidoreductases / metabolism
  • Amino Acid Sequence
  • Azurin / metabolism
  • Catalytic Domain
  • Glucose 1-Dehydrogenase
  • Glucose Dehydrogenases / metabolism
  • Ligands
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Protein Structure, Tertiary
  • Pseudomonas putida / chemistry*
  • Pseudomonas putida / metabolism
  • Sequence Alignment


  • Ligands
  • Azurin
  • Alcohol Oxidoreductases
  • Glucose Dehydrogenases
  • Glucose 1-Dehydrogenase
  • alcohol dehydrogenase (acceptor)

Associated data

  • PDB/1KV9