The Q(o)-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton

FEBS Letters

Volumn 450, Issue 3, 1999, Pages 245-250

  Schoepp, Barbara ^a,b   Brugna, Myriam ^a   Riedel, Astrid ^c   Nitschke, Wolfgang ^a,b   Kramer, David M ^b,d  

^a AIX MARSEILLE UNIVERSITÉ   (France)

^b UNIVERSITY OF FREIBURG   (Germany)

^c UNIVERSITY OF REGENSBURG   (Germany)

^d Institute of Biological Chemistry   (United States)

Author keywords

DBMIB; EPR; Redox linked proton; Rieske; Rieske protein's domain movement

Indexed keywords

2,5 DIBROMO 6 ISOPROPYL 3 METHYLBENZOQUINONE; CYTOCHROME; IRON SULFUR PROTEIN; PROTON; ASCORBIC ACID; CYTOCHROME B; CYTOCHROME B6F; RIESKE IRON-SULFUR PROTEIN; UBIQUINOL CYTOCHROME C REDUCTASE;

ARTICLE; CHLOROPLAST; ELECTRON SPIN RESONANCE; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN DOMAIN; SPINACH; BINDING SITE; CHEMISTRY; DRUG ANTAGONISM; METABOLISM; OXIDATION REDUCTION REACTION;

ASCORBIC ACID; BINDING SITES; CHLOROPLASTS; CYTOCHROME B GROUP; CYTOCHROME B6F COMPLEX; DIBROMOTHYMOQUINONE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT COMPLEX III; IRON-SULFUR PROTEINS; OXIDATION-REDUCTION; PROTONS;

EID: 0032587408     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)00511-6     Document Type: Article

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