Study of the reactivity of quinohemoprotein alcohol dehydrogenase with heterocycle-pentacyanoferrate(III) complexes and the electron transfer path calculations

Lidija Tetianec, Marius Dagys, Juozas Kulys, Arturas Ziemys, Rolandas Meskys

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The reactivity of alcohol dehydrogenase IIG (ADH IIG) from Pseudomonas putida HK5 with new heterocycle-pentacyanoferrate(III) complexes and hexacyanoferrate(III) was determined at pH 7.2. The pentacyanoferrate(III) complexes contained imidazole, pyrazole, pyridine, their derivatives and 2-aminobenzothiazole as the sixth ligand. The largest reactivity of the complexes with ADH IIG was estimated for the complex containing pyridine. An apparent bimolecular constant (k ox ) for this complex was 8.7 × 105 M-1s-1. The lowest value of k ox was estimated for the complex with benzotriazole (k ox = 3.1 × 104 M-1s-1). The investigation of the hexacyanoferrate(III) enzymatic reduction rate at different ionic strength gave a single negative charge of reduced ADH IIG. Docking calculations revealed two binding sites of the complexes in ADH-IIG structure. The first one is located at the entrance to the PQQ pocket, and the second is at the site of cytochrome domain. The calculations of electron transfer (ET) path indicated that the most effective ET takes place from heme to the complex docked at the entrance to the PQQ pocket. This shortest path is constructed of amino acids Ser607 and Cys606.

Original languageEnglish (US)
Pages (from-to)502-517
Number of pages16
JournalCentral European Journal of Biology
Volume2
Issue number4
DOIs
StatePublished - Sep 2007

Keywords

  • Alcohol dehydrogenase
  • Electron acceptor
  • Enzyme
  • Kinetics
  • Pentacyanoferrate
  • Quinohemoprotein

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Neuroscience(all)

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