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Literature summary for 7.4.2.4 extracted from

  • Buchert, F.; Schober, Y.; Roempp, A.; Richter, M.L.; Forreiter, C.
    Reactive oxygen species affect ATP hydrolysis by targeting a highly conserved amino acid cluster in the thylakoid ATP synthase gamma subunit (2012), Biochim. Biophys. Acta, 1817, 2038-2048.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C199A/C205A ratio of MgATPase activity in reduced/oxidized state is 0.79, compared to 1.7 in wild-type Spinacia oleracea
C89A ratio of MgATPase activity in reduced/oxidized state is 1.39, compared to 1.7 in wild-type Spinacia oleracea
M231L ratio of MgATPase activity in reduced/oxidized state is 1.0, compared to 1.7 in wild-type Spinacia oleracea
M23L/M279L/M282L ratio of MgATPase activity in reduced/oxidized state is 0.99, compared to 1.7 in wild-type Spinacia oleracea
M23L/M279L/M282L/C89A ratio of MgATPase activity in reduced/oxidized state is 1.08, compared to 1.7 in wild-type Spinacia oleracea
M279L/M282L ratio of MgATPase activity in reduced/oxidized state is 0.96, compared to 1.7 in wild-type Spinacia oleracea

Inhibitors

Inhibitors Comment Organism Structure
reactive oxygen species reactive oxygen species dramatically decrease ATP synthesis in situ and affect the coupling factor CF1 portion in vitro. A conserved cluster of three methionines and a cysteine on the chloroplast gamma subunit are oxidized by reactive oxygen species. These residues are exclusive catalytic targets for hydrogen peroxide and singlet oxygen, although additional unknown amino acid targets might be involved in the latter reaction. The cluster is tightly integrated in catalytic turnover since mutants vary in MgATPase rates, stimulation by sulfite and chloroplast-specific gamma subunit redox-modulation Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid
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Spinacia oleracea 9579
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Organism

Organism UniProt Comment Textmining
Spinacia oleracea
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-
-