Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1837, Issue 10, Pages 1691-1698Publisher
ELSEVIER
DOI: 10.1016/j.bbabio.2014.07.021
Keywords
Hydrogenases; Electron transport; Sulfur metabolism; Thiocapsa roseopersicina; Photosynthesis; Photosynthetic bacteria
Categories
Funding
- European Union
- State of Hungary
- State of Hungary - European Social Fund [TAMOP 4.2.4. A/2-11-1-2012-0001, TAMOP-4.1.1.C-12/1IKONV-2012-0012]
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Thiocapsa. roseopersicina BBS has four active [NiFe] hydrogenases, providing an excellent opportunity to examine their metabolic linkages to the cellular redox processes. Hyn is a periplasmic membrane-associated hydrogenase harboring two additional electron transfer subunits: Isp1 is a transmembrane protein, while Isp2 is located on the cytoplasmic side of the membrane. In this work, the connection of HynSL to various electron transport pathways is studied. During photoautotrophic growth, electrons, generated from the oxidation of thiosulfate and sulfur, are donated to the photosynthetic electron transport chain via cytochromes. Electrons formed from thiosulfate and sulfur oxidation might also be also used for Hyn-dependent hydrogen evolution which was shown to be light and proton motive force driven. Hyn-linked hydrogen uptake can be promoted by both sulfur and nitrate. The electron flow from/to HynSL requires the presence of Isp2 in both directions. Hydrogenase-linked sulfur reduction could be inhibited by a Q(B) site competitive inhibitor, terbutryne, suggesting a redox coupling between the Hyn hydrogenase and the photosynthetic electron transport chain. Based on these findings, redox linkages of Hyn hydrogenase are modeled. (C) 2014 Elsevier B.V. All rights reserved.
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