Table 2.
bc1 mutants | Bovine equivalent | Photosynthetic growth | Specific activity* |
Km | Note | Source | |
---|---|---|---|---|---|---|---|
Purified Rsbc1 | Chromatophore | ||||||
Bovine bc1 | — | 20.0 | — | N/A | Having a KS dyad in cyt b with two H-bonds to ISP | This work | |
Wt Rsbc1 | +++++ | 2.5 | 2.2 | 1.56 | Having no KS dyad still with two H-bonds to ISP | This work | |
KS dyad mutants | |||||||
G167S | S151 | +++++ | 2.4 | 1.9 | 1.50 | Forming a KS dyad, presumably leading to two H-bonds | This work |
S322A | ++++† | 0.76 | 0.67 | 2.00 | Single mutation in the ef1 insertion in rsbc1 | This work | |
Δ(309–326) | ++++† | 0.48 | 0.46 | 1.45 | Deletion mutant of the ef1 insertion in rsbc1 | This work | |
Δ(309–326)/ G167S | ++++† | 0.46 | 0.34 | 1.39 | Double mutations mimicking bovine bc1 with the KS dyad | This work | |
SC mutant | |||||||
W142R,K,T,S | W141 | — | — | — | — | Respiration incapable in yeast, c+c1 reduction kinetics severely affected | Ref. 25 |
T160S,Y | T144 | — | — | — | — | 70–80% lower activity in rsbc1 | Ref. 26 |
292F | I268 | — | — | — | — | Incapable of photosynthetic growth in R.s., affecting QH2 oxidation | Ref. 27 |
L282F | L281 | — | — | — | — | Respiration incapable in yeast | Ref. 28 |
L305A,D | L281 | — | — | — | — | Slow QH2 oxidation in rsbc1 | Ref. 27 |
K329A | K287 | ++++† | 0.9 | 0.8 | 1.40 | Mutant that has lowered QH2 oxidation activity in rsbc1 and changes the shape complementarity | This work and ref. 27 |
*Enzymatic activity is expressed as μmol of cyt c reduced per min/nmol cyt b at room temperature. The concentration of cyt c in assay mixture is 50 μM.
†Delayed by >12 h.