Applied Microbiology and Biotechnology

, Volume 58, Issue 1, pp 13–22

Quinoproteins: structure, function, and biotechnological applications

  •  K. Matsushita
  •  H. Toyama
  •  M. Yamada
  •  O. Adachi
Mini-Review

DOI: 10.1007/s00253-001-0851-1

Cite this article as:
Matsushita, K., Toyama, H., Yamada, M. et al. Appl Microbiol Biotechnol (2002) 58: 13. doi:10.1007/s00253-001-0851-1

Abstract.

A new class of oxidoreductase containing an amino acid-derived o-quinone cofactor, of which the most typical is pyrroloquinoline quinone (PQQ), is called quinoproteins, and has been recognized as the third redox enzyme following pyridine nucleotide- and flavin-dependent dehydrogenases. Some quinoproteins include a heme c moiety in addition to the quinone cofactor in the molecule and are called quinohemoproteins. PQQ-containing quinoproteins and quinohemoproteins have a common structural basis, in which PQQ is deeply embedded in the center of the unique superbarrel structure. Increased evidence for the structure and function of quinoproteins has revealed their unique position within the redox enzymes with respect to catalytic and electron transfer properties, and also to physiological and energetic function. The peculiarities of the quinoproteins, together with their unique substrate specificity, have encouraged their biotechnological application in the fields of biosensing and bioconversion of useful compounds, and also to environmental treatment.

Copyright information

© Springer-Verlag 2001

Authors and Affiliations

  •  K. Matsushita
    • 1
  •  H. Toyama
    • 1
  •  M. Yamada
    • 1
  •  O. Adachi
    • 1
  1. 1.Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi, Yamaguchi 753–8515, Japan