Interaction of stigmatellin and DNP-INT with the Rieske iron-sulfur center of the chloroplast cytochrome b6-f complex.
Stigmatellin and DNP-INT are effective inhibitors of the catalytic activity of the plastoquinol-plastocyanin oxidoreductase complex (cytochrome b6-f complex). Both inhibitors alter the EPR spectrum of the Rieske iron-sulfur center but do not produce band-shifts of cytochrome b-563. The midpoint redox potential of the Rieske center is unaffected by either inhibitor, although both alter the DBMIB-induced g-value shifts of the Rieske center. The results are considered in terms of binding domains for inhibitors in the cytochrome b6-f complex.
D001665:Binding Sites; D002736:Chloroplasts / Q000502:physiology*; D003573:Cytochrome b Group / Q000378:metabolism*; D045346:Cytochrome b6f Complex; D004578:Electron Spin Resonance Spectroscopy; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D008667:Metalloproteins / Q000378:metabolism*; D009578:Nitrobenzenes / Q000494:pharmacology*; D010084:Oxidation-Reduction; D011090:Polyenes / Q000378:metabolism; D014301:Trinitrobenzenes / Q000494:pharmacology*
D003573:Cytochrome b Group; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D009578:Nitrobenzenes; D011090:Polyenes; D014301:Trinitrobenzenes; C026642:2-iodo-6-isopropyl-3-methyl-2',4,4'-trinitrodiphenyl ether; D045346:Cytochrome b6f Complex; C041573:stigmatellin