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. Author manuscript; available in PMC: 2009 Jul 1.

Published in final edited form as: Biochim Biophys Acta. 2008 May 1;1777(7-8):1001–1019. doi: 10.1016/j.bbabio.2008.04.037

Fig. 4 — a) Typical curves showing the kinetics of heme b_H reduction in WT in the presence of antimycin. Similar sets of data were taken for each strain, all of which had similar maximal rates. Myxothiazol concentrations are indicated to the right of each curve. b) Fraction of heme b_H reduced at 20 ms (expressed as %) in the presence of Q_i-site inhibitor antimycin A, as a function of inhibitor concentration. The system was excited with a xenon flash (~5 µs at half-height) and the reduction of b_H monitored from the difference kinetics measured at 561–569 nm. Ambient redox potential was poised at ~100 mV (QH₂ oxidation close to maximal). Strains are indicated by labels; bc₁ complex in the range 70–220 nM.

Fig. 4 — a) Typical curves showing the kinetics of heme b_H reduction in WT in the presence of antimycin. Similar sets of data were taken for each strain, all of which had similar maximal rates. Myxothiazol concentrations are indicated to the right of each curve. b) Fraction of heme b_H reduced at 20 ms (expressed as %) in the presence of Q_i-site inhibitor antimycin A, as a function of inhibitor concentration. The system was excited with a xenon flash (~5 µs at half-height) and the reduction of b_H monitored from the difference kinetics measured at 561–569 nm. Ambient redox potential was poised at ~100 mV (QH₂ oxidation close to maximal). Strains are indicated by labels; bc₁ complex in the range 70–220 nM.