Effect of mutations of arginine 94 on proton pumping, electron transfer, and superoxide anion generation in cytochrome b of the bc₁ complex from Rhodobacter sphaeroides.

VOLUME 288 (2013) PAGES 1047–1054

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The proton translocation rate of Fig. 3 was monitored at A₄₅₇ (y axis) and not A₅₅₆ as shown in the original figure.

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Fig. 7 should be modified as shown below.

FIGURE 7.

Electron transfer activity changes in the wild-type and mutant bc₁ complexes under aerobic or anaerobic conditions. The activity of wild-type bc₁ under the aerobic conditions is referenced as 100%. Data represent an average of three experiments. Error bars indicate S.D.

Fig. 8 should be modified as shown below.

FIGURE 8.

Schematic depiction of the transfer of the two electrons and two protons of a ubiquinol at the Q_P pocket when oxidized in the bc₁ complex. The first electron and proton are in green, and the second electron and proton are in red. The purple arrow indicates oxygen molecules that are diffused to the Q_P pocket. Dashed arrows indicate plausible electron, proton, and superoxide transfer routes. Q_P and Q_N denote quinol oxidation and the quinone reduction pocket. QH₂, ubiquinol; TM, transmembrane region; ISP, Rieske iron-sulfur protein.