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Cited by 109Microbial metabolism and enzyme functionEnzyme Structure and FunctionMetal-Catalyzed Oxygenation Mechanisms

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Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology

Toyama, Hirohide, Mathews, F.Scott, Adachi, Osao, Matsushita, Kazunobu·2004·Archives of Biochemistry and Biophysics
DOI 10.1016/j.abb.2004.03.037
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Abstract

Quino(hemo)protein alcohol dehydrogenases (ADH) that have pyrroloquinoline quinone (PQQ) as the prosthetic group are classified into 3 groups, types I, II, and III. Type I ADH is a simple quinoprotein having PQQ as the only prosthetic group, while type II and type III ADHs are quinohemoprotein having heme c as well as PQQ in the catalytic polypeptide. Type II ADH is a soluble periplasmic enzyme and is widely distributed in Proteobacteria such as Pseudomonas, Ralstonia, Comamonas, etc. In contrast, type III ADH is a membrane-bound enzyme working on the periplasmic surface solely in acetic acid bacteria. It consists of three subunits that comprise a quinohemoprotein catalytic subunit, a triheme cytochrome c subunit, and a third subunit of unknown function. The catalytic subunits of all the quino(hemo)protein ADHs have a common structural motif, a quinoprotein-specific superbarrel domain, where PQQ is deeply embedded in the center. In addition, in the type II and type III ADHs this subunit contains a unique heme c domain. Various type II ADHs each have a unique substrate specificity, accepting a wide variety of alcohols, as is discussed on the basis of recent X-ray crystallographic analyses. Electron transfer within both type II and III ADHs is discussed in terms of the intramolecular reaction from PQQ to heme c and also from heme to heme, and in terms of the intermolecular reaction with azurin and ubiquinone, respectively. Unique physiological functions of both types of quinohemoprotein ADHs are also discussed.

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Metadata

Authors
Toyama, H., Mathews, F. S., Adachi, O., & Matsushita, K.
Affiliations
Yamaguchi University (JP)
Corresponding author
Matsushita, Kazunobu
ORCID
Venue
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Published
2004-08
Volume
428
Issue
1
Pages
10-21
ISSN
0003-9861 (ISSN-L)
DOI
10.1016/j.abb.2004.03.037
OpenAlex
W2050010239
Cited by
109
References
0
Citations by year
2026: 2 · 2025: 5 · 2024: 3 · 2023: 3 · 2022: 3 · 2021: 6 · 2020: 3 · 2019: 5 · 2018: 9 · 2017: 8 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 5 · 2012: 4
FWCI
0.46
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Archives of Biochemistry and Biophysics (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords
pyrroloquinoline quinone, heme c, quinoproteins, substrate specificity, electron transfer, azurin, coenzyme Q10, periplasmic enzymes, membrane-bound enzyme, acetic acid bacteria, Pseudomonas, Proteobacteria, enzyme structure
MeSH terms
Alcohol Oxidoreductases, Alcohols, Amino Acid Sequence, Electron Transport, Enzyme Activation, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Conformation, Species Specificity, Structure-Activity Relationship, Sequence Homology, Amino Acid, Proteobacteria, PQQ Cofactor

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CoChat. (2026). Citation check: Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology. https://app.cochat.ai/papers/10.1016/j.abb.2004.03.037
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Toyama, H., Mathews, F. S., Adachi, O., & Matsushita, K. (2004). Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology. Archives of Biochemistry and Biophysics. https://doi.org/10.1016/j.abb.2004.03.037