Structural properties, functional states and physiological roles of hydrogenase in photosynthetic bacteria

K. Kovács, Csaba Bagyinka

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The membrane-bound hydrogenase from Thiocapsa roseopersicina is composed of two subunits and contains two Fe-S centres and one Ni per molecule. The enzyme resists heat and proteolytic degradation, its activity is retained under SDS-PAGE conditions. The location of the metal atoms on the subunits has been determined by proton-induced X-ray emission (PIXE). A revised hydrogenase model which concurs with the new data is suggested. The orientation of the enzyme in the photosynthetic membrane and its ability to generate membrane potential suggest that hydrogenase can play a significant role in the energetics of these bacteria. A possible link between nitrogen fixation, photosynthetic electron transport and hydrogenase is proposed.

Original languageEnglish
Pages (from-to)407-411
Number of pages5
JournalFEMS Microbiology Letters
Volume87
Issue number3-4
DOIs
Publication statusPublished - 1991

Fingerprint

Hydrogenase
Bacteria
Thiocapsa roseopersicina
Nitrogen Fixation
Membranes
Enzymes
Electron Transport
Membrane Potentials
Protons
Polyacrylamide Gel Electrophoresis
Hot Temperature
Metals
X-Rays

Keywords

  • Active states
  • Bioenergetics
  • Hydrogenase
  • Membrane potential
  • Subunit structure
  • Thiocapsa roseopersicina

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

Structural properties, functional states and physiological roles of hydrogenase in photosynthetic bacteria. / Kovács, K.; Bagyinka, Csaba.

In: FEMS Microbiology Letters, Vol. 87, No. 3-4, 1991, p. 407-411.

Research output: Contribution to journalArticle

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