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Sökning: WFRF:(Robert Olsson Mats Joakim)

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2.
  • Abdallah, Jalal, et al. (författare)
  • Study of energy response and resolution of the ATLAS Tile Calorimeter to hadrons of energies from 16 to 30 GeV
  • 2021
  • Ingår i: European Physical Journal C. - : Springer Science and Business Media LLC. - 1434-6044 .- 1434-6052. ; 81:6
  • Tidskriftsartikel (refereegranskat)abstract
    • Three spare modules of the ATLAS Tile Calorimeter were exposed to test beams from the Super Proton Synchrotron accelerator at CERN in 2017. The detector’s measurements of the energy response and resolution to positive pions and kaons, and protons with energies ranging from 16 to 30 GeV are reported. The results have uncertainties of a few percent. They were compared to the predictions of the Geant4-based simulation program used in ATLAS to estimate the response of the detector to proton-proton events at the Large Hadron Collider. The determinations obtained using experimental and simulated data agree within the uncertainties.
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3.
  • Sirijovski, Nick, et al. (författare)
  • ATPase activity associated with the magnesium chelatase H-subunit of the chlorophyll biosynthetic pathway is an artefact
  • 2006
  • Ingår i: Biochemical Journal. - 0264-6021. ; 400, s. 477-484
  • Tidskriftsartikel (refereegranskat)abstract
    • Magnesium chelatase inserts Mg2+ into protoporphyrin IX and is the first unique enzyme of the chlorophyll biosynthetic pathway. It is a heterotrimeric enzyme, composed of I- (40 kDa), D- (70 kDa) and H- (140 kDa) subunits. The I- and D-proteins belong to the family of AAA(+) (ATPases associated with various cellular activities), but only I-subunit hydrolyses ATP to ADP. The D-subunits provide a platform for the assembly of the I-subunits, which results in a two-tiered hexameric ring complex. However, the D-subunits are unstable in the chloroplast unless ATPase active I-subunits are present. The H-subunit binds protoporphyrin and is suggested to be the catalytic subunit. Previous studies have indicated that the H-subunit also has ATPase activity, which is in accordance with an earlier suggested two-stage mechanism of the reaction. In the present study, we demonstrate that gel filtration chromatography of affinity-purified Rhodobacter capsulatus H-subunit produced in Escherichia coli generates a high- and a low-molecular-mass fraction. Both fractions were dominated by the H-subunit, but the ATPase activity was only found in the high-molecular-mass fraction and magnesium chelatase activity was only associated with the low-molecular-mass fraction. We demonstrated that light converted monomeric low-molecular-mass H-subunit into high-molecular-mass aggregates. We conclude that ATP utilization by magnesium chelatase is solely connected to the I-subunit and suggest that a contaminating E. coli protein, which binds to aggregates of the H-subunit, caused the previously reported ATPase activity of the H-subunit.
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