Reconstitution of the heliobacterial photochemical reaction center and cytochrome c553 into a proteoliposome system View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12-14

AUTHORS

William A. Johnson, Kevin E. Redding

ABSTRACT

The heliobacterial reaction center (HbRC) is the simplest known photochemical reaction center, in terms of its polypeptide composition. In the heliobacterial cells, its electron donor is a cytochrome (cyt) c553 attached to the membrane via a covalent linkage with a diacylglycerol. We have reconstituted purified HbRC into liposomes mimicking the phospholipid composition of heliobacterial membranes. We also incorporated a lipid with a headgroup containing Ni(II):nitrilotriacetate (NTA) to provide a binding site for the soluble version of the heliobacterial cyt c553 in which the N-terminal membrane attachment site is replaced by a hexahistidine tag. The HbRC was inserted into the liposomes with the donor side preferentially exposed to the exterior; this bias increased to nearly 100% with higher concentrations (≥ 10 mol%) of the Ni(II)-NTA lipid in the membrane, and is most likely due to the net negative charge of the surface of the membrane. The HbRC in proteoliposomes without the Ni(II)-NTA lipid exhibited normal charge separation and subsequent charge recombination of the P800+FX− state in 15 ms; however, the oxidized primary donor (P800+) was not significantly reduced by added H6-cyt c553. In contrast, with proteoliposomes containing the Ni(II)-NTA lipid, addition of H6-cyt c553 resulted in a new kinetic component resulting from fast reduction (2–5 ms) of P800+ by H6-cyt c553. The contribution of this kinetic component varied with the concentration of added H6-cyt c553 and could represent 80% or more of the total P800+ decay. Thus, the HbRC and its interaction with its native electron donor have been reconstituted into an artificial membrane system. More... »

PAGES

241-250

References to SciGraph publications

  • 2012-03-02. Purification of the photosynthetic reaction center from Heliobacterium modesticaldum in PHOTOSYNTHESIS RESEARCH
  • 2013-12-07. Modulation of the fluorescence yield in heliobacterial cells by induction of charge recombination in the photosynthetic reaction center in PHOTOSYNTHESIS RESEARCH
  • 2018-03-12. Light-driven quinone reduction in heliobacterial membranes in PHOTOSYNTHESIS RESEARCH
  • 2008-11-25. Effect of monogalactosyldiacylglycerol on the interaction between photosystem II core complex and its antenna complexes in liposomes of thylakoid lipids in PHOTOSYNTHESIS RESEARCH
  • 1994-07. Lipids of heliobacteria are characterised by a high proportion of monoenoic fatty acids with variable double bond positions in PHOTOSYNTHESIS RESEARCH
  • 2014-02-21. Expression and characterization of cytochrome c553 from Heliobacterium modesticaldum in PHOTOSYNTHESIS RESEARCH
  • 2003-06. Discovery and characterization of electron transfer proteins in the photosynthetic bacteria in PHOTOSYNTHESIS RESEARCH
  • 2002-02. Electron donation from membrane-bound cytochrome c to the photosynthetic reaction center in whole cells and isolated membranes of Heliobacterium gestii in PHOTOSYNTHESIS RESEARCH
  • 1995-04. Heliobacterium modesticaldum, sp. nov., a thermophilic heliobacterium of hot springs and volcanic soils in ARCHIVES OF MICROBIOLOGY
  • 1999-09. Laser-flash absorption spectroscopy study of the competition between ferredoxin and flavodoxin photoreduction by Photosystem I in Synechococcus sp. PCC 7002: Evidence for a strong preference for ferredoxin in PHOTOSYNTHESIS RESEARCH
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s11120-019-00695-w

    DOI

    http://dx.doi.org/10.1007/s11120-019-00695-w

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1123388461

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/31838634


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