Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Binding Sites
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Chloroplasts / physiology*
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Cytochrome b Group / metabolism*
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Cytochrome b6f Complex
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Electron Spin Resonance Spectroscopy
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Iron-Sulfur Proteins / metabolism*
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Metalloproteins / metabolism*
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Nitrobenzenes / pharmacology*
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Oxidation-Reduction
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Polyenes / metabolism
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Trinitrobenzenes / pharmacology*
Substances
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Cytochrome b Group
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Iron-Sulfur Proteins
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Metalloproteins
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Nitrobenzenes
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Polyenes
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Trinitrobenzenes
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2-iodo-6-isopropyl-3-methyl-2',4,4'-trinitrodiphenyl ether
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Cytochrome b6f Complex
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stigmatellin