7.1.1.3 D135E the mutant shows 45% activity compared to the wild type enzyme 714130 7.1.1.3 D135K the mutant is deficient in proton pumping (23% activity compared to the wild type enzyme) 714135 7.1.1.3 D135N the mutant is deficient in proton pumping (45% activity compared to the wild type enzyme) 714135 7.1.1.3 D135N the mutant shows 45% activity compared to the wild type enzyme, with proton pumping decoupled from the electron-transfer activity -, 714130 7.1.1.3 D135N the mutations specifically eliminates the CuB center from the oxidase complex 715399 7.1.1.3 D188N the mutant possesses 100% copper and 81% cytochrome o compared to the wild type enzyme 715399 7.1.1.3 D188N the mutant shows 53% activity compared to the wild type enzyme 714130 7.1.1.3 D256N the mutant possesses 103% copper and 74% cytochrome o compared to the wild type enzyme 715399 7.1.1.3 D256N the mutant shows 25% activity compared to the wild type enzyme -, 714130 7.1.1.3 D36V the mutant of subunit III shows 160% activity compared to the wild type enzyme 741988 7.1.1.3 D407N the mutant shows 31% activity compared to the wild type enzyme -, 714130 7.1.1.3 D407N the mutation affects the CO-binding by the heme-copper binuclear center -, 715399 7.1.1.3 D75E 135% activity compared to the wild type enzyme 714308 7.1.1.3 D75E the mutant shows 48% activity with ubiquinol-1 and 88% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 D75H 4% activity compared to the wild type enzyme 714308 7.1.1.3 D75H mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials 749941 7.1.1.3 D75N inactive 714308 7.1.1.3 D75N the mutation inhibits activity by 99% 716311 7.1.1.3 D75R inactive 714308 7.1.1.3 E164A the mutant of subunit I shows 28% activity compared to the wild type enzyme 741988 7.1.1.3 E164K the mutant of subunit I shows 54% activity compared to the wild type enzyme 741988 7.1.1.3 E259A the mutant of subunit II shows 135% activity compared to the wild type enzyme 741988 7.1.1.3 E259K the mutant of subunit II shows 97% activity compared to the wild type enzyme 741988 7.1.1.3 E286A inactive -, 714130, 715000 7.1.1.3 E286C the mutant shows 3% activity compared to the wild type enzyme as a result of the inhibition of proton transfer from the D-channel -, 714331 7.1.1.3 E286C the mutant still reduces oxygen to oxidize ubiquinol, transporting chemical protons across the membrane in the process, but is unable to pump protons 741989 7.1.1.3 E286D the mutant does not show significant perturbations on the redox metal centers even though it is still inactive 715399 7.1.1.3 E286D the mutant retains 31% of the wild type activity -, 715000 7.1.1.3 E286Q the mutant shows 4% activity compared to the wild type enzyme and is unable to bind azide ions -, 715000 7.1.1.3 E286Q the mutant shows 69% activity compared to the wild type enzyme -, 714130 7.1.1.3 E286Q the mutations specifically eliminates the CuB center from the oxidase complex -, 715399 7.1.1.3 E445A heme b595 is present in the E445A mutant. Formation of the oxoferryl state in the mutant is about 100fold slower than in the wild type enzyme. The E445A substitution does not affect intraprotein electron re-equilibration after the photolysis of CO bound to ferrous heme d in the one-electron-reduced enzyme. The mutation does not affect membrane potential generation coupled to intramolecular electron redistribution between hemes d2+ and b558 -, 716735 7.1.1.3 E540Q the mutation affects the CO-binding by the heme-copper binuclear center 715399 7.1.1.3 F112L the mutation does not affect the in vivo activity 714141 7.1.1.3 F113L the mutation does not affect the in vivo activity -, 714141 7.1.1.3 F138G the mutant shows 63% proton-translocating activity compared to the wild type enzyme 714135 7.1.1.3 F138R the mutant shows 55% proton-translocating activity compared to the wild type enzyme 714135 7.1.1.3 F165A the mutant of subunit I shows 37% activity compared to the wild type enzyme 741988 7.1.1.3 F208L the mutation does not affect the in vivo activity 714141 7.1.1.3 F295L the mutation does not affect the in vivo activity -, 714141 7.1.1.3 F29I the mutant of subunit III shows 115% activity compared to the wild type enzyme 741988 7.1.1.3 F336L the mutation does not affect the in vivo activity 714141 7.1.1.3 F347L the mutation does not affect the in vivo activity -, 714141 7.1.1.3 F348L 4.8% activity compared to the wild type enzyme 714141 7.1.1.3 F391L the mutation does not affect the in vivo activity 714141 7.1.1.3 F415W the mutation does not affect the in vivo activity 714141 7.1.1.3 F420L the mutation does not affect the in vivo activity -, 714141 7.1.1.3 F93A the mutant shows 37% activity with ubiquinol-1 and 102% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 F93Y mutant exhibits good electrocatalytic performance and a well-defined sigmoidal i-V curve. Compared to wild-type, the half-wave potential is downshifted by up to 40 mV 749941 7.1.1.3 F93Y the mutant shows 81% activity with ubiquinol-1 and 107% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 G132A the mutant shows wild type proton-translocation activity (113% activity compared to the wild type enzyme) 714135 7.1.1.3 G132D/D135N the mutant shows 66% proton-translocating activity compared to the wild type enzyme 714135 7.1.1.3 G132R the mutant shows wild type proton-translocation activity 714135 7.1.1.3 H333C nonfunctional enzyme -, 714132 7.1.1.3 H333L the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme -, 714132 7.1.1.3 H333N nonfunctional enzyme -, 714132 7.1.1.3 H333Q nonfunctional enzyme -, 714132 7.1.1.3 H334L the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme -, 714132 7.1.1.3 H334M nonfunctional enzyme 714132 7.1.1.3 H98F mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials 749941 7.1.1.3 H98N 1% activity compared to the wild type enzyme 714308 7.1.1.3 H98N the mutant shows 3% activity with ubiquinol-1 and 10% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 H98N the mutation inhibits activity by 97% 716311 7.1.1.3 H98S 2% activity compared to the wild type enzyme 714308 7.1.1.3 H98T 1% activity compared to the wild type enzyme 714308 7.1.1.3 H98T the mutant shows 4% activity with ubiquinol-1 and 9% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 I102W mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials 749941 7.1.1.3 K25L the mutant of subunit III shows75 % activity compared to the wild type enzyme 741988 7.1.1.3 K362D/Dl35K the mutant is devoid of redox activity 714135 7.1.1.3 K362L catalytically inactive 714131 7.1.1.3 K362M catalytically inactive -, 714131 7.1.1.3 K362Q catalytically inactive -, 714131 7.1.1.3 K362Q the mutation affects the CO-binding by the heme-copper binuclear center 715399 7.1.1.3 K55Q the mutant possesses 100% copper and 73% cytochrome o compared to the wild type enzyme -, 715399 7.1.1.3 L160W the mutant shows 58% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 L171A the mutant of subunit I shows 79% activity compared to the wild type enzyme 741988 7.1.1.3 M353A the mutant shows substantial activity 714131 7.1.1.3 additional information plasmid-based overexpression of cyoBACD leads to increased growth rates and growth yields, both in the wild-type and the DELTAcyoBACD mutant, suggesting that cytochrome bo3 might be a rate-limiting factor of the respiratory chain 725289 7.1.1.3 N124D the mutant is deficient in proton pumping (56% activity compared to the wild type enzyme) 714135 7.1.1.3 N124D/D135N the mutant shows 21% proton-translocating activity compared to the wild type enzyme 714135 7.1.1.3 N124H the mutant is deficient in proton pumping (16% activity compared to the wild type enzyme) 714135 7.1.1.3 N142D the mutant is deficient in proton pumping (48% activity compared to the wild type enzyme) 714135 7.1.1.3 N142D/D135N the mutant shows 33% proton-translocating activity compared to the wild type enzyme 714135 7.1.1.3 N142Q the mutant shows wild type proton-translocation activity (109% activity compared to the wild type enzyme) 714135 7.1.1.3 N142V the mutant is deficient in proton pumping (22% activity compared to the wild type enzyme) 714135 7.1.1.3 N157V the mutant shows 23% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 P128A the mutant shows wild type proton-translocation activity (115% activity compared to the wild type enzyme) 714135 7.1.1.3 P128D/D135N inactive 714135 7.1.1.3 P139E/D135N the mutant shows 95% proton-translocating activity compared to the wild type enzyme 714135 7.1.1.3 P358A the mutant shows substantial activity 714131 7.1.1.3 Pl39A the mutant shows wild type proton-translocation activity (67% activity compared to the wild type enzyme) 714135 7.1.1.3 Pl39E the mutant shows wild type proton-translocation activity (46% activity compared to the wild type enzyme) 714135 7.1.1.3 Q101A mutant exhibits good electrocatalytic performance and a well-defined sigmoidal i-V curve. Compared to wild-type, the half-wave potential is downshifted by up to 40 mV 749941 7.1.1.3 Q101A the mutant shows 26% activity with ubiquinol-1 and 82% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 Q101E the mutant shows 55% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 Q101L mutant exhibits good electrocatalytic performance and a well-defined sigmoidal i-V curve. Compared to wild-type, the half-wave potential is downshifted by up to 40 mV 749941 7.1.1.3 Q101L the mutant shows 11% activity with ubiquinol-1 and 58% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 Q101M the mutant shows 51% activity with ubiquinol-1 and 72% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 Q101N 5% activity compared to the wild type enzyme 714308 7.1.1.3 Q101N the mutant shows 10% activity with ubiquinol-1 and 61% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 Q101N the mutation inhibits activity by 75% and causes a 10fold increase in the apparent KM for ubiquinol-1 716311 7.1.1.3 Q101T the mutant shows 27% activity with ubiquinol-1 and 62% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 Q167A the mutant of subunit I shows 57% activity compared to the wild type enzyme 741988 7.1.1.3 Q167K the mutant of subunit I shows 75% activity compared to the wild type enzyme 741988 7.1.1.3 Q195L the mutant of subunit I shows 119% activity compared to the wild type enzyme 741988 7.1.1.3 Q82A the mutant shows 88% activity with ubiquinol-1 and no activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 R134P the mutant shows 112% proton-translocating activity compared to the wild type enzyme 714135 7.1.1.3 R176A the mutant of subunit III shows 70% activity compared to the wild type enzyme 741988 7.1.1.3 R257Q the mutations specifically eliminates the CuB center from the oxidase complex 715399 7.1.1.3 R481L nonfunctional mutant 714169 7.1.1.3 R481Q the mutant is fully functional 714169 7.1.1.3 R481Q the mutant possesses 91% copper and 73% cytochrome o compared to the wild type enzyme 715399 7.1.1.3 R482Q the mutant possesses 82% copper and 100% cytochrome o compared to the wild type enzyme 715399 7.1.1.3 R71D inactive 714308 7.1.1.3 R71D/D75R inactive 714308 7.1.1.3 R71H mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials 749941 7.1.1.3 R71K inactive 714308 7.1.1.3 R71L the mutation inhibits activity by 99% 716311 7.1.1.3 R71Q inactive 714308 7.1.1.3 R71Q the mutant shows 3% activity with ubiquinol-1 and 8% activity with ubiquinol-2 compared to the wild type enzyme 742754 7.1.1.3 R71Q the mutation inhibits activity by 99% 716311 7.1.1.3 R80Q the mutation causes loss of a diagnostic peak for low-spin heme b in the 77 K redox difference spectrum -, 715399 7.1.1.3 S177A the mutant of subunit I shows 91% activity compared to the wild type enzyme 741988 7.1.1.3 T168A the mutant of subunit I shows 118% activity compared to the wild type enzyme 741988 7.1.1.3 T247V the mutant of subunit I shows 173% activity compared to the wild type enzyme 741988 7.1.1.3 T352A catalytically inactive -, 714131 7.1.1.3 T352N the mutant shows substantial activity -, 714131 7.1.1.3 T352S the mutant shows substantial activity 714131 7.1.1.3 T359A catalytically inactive -, 714131 7.1.1.3 T359S the mutant shows almost wild type activity 714131 7.1.1.3 W136A the mutant of subunit II shows 89% activity compared to the wild type enzyme 741988 7.1.1.3 W136K the mutant of subunit II shows 105% activity compared to the wild type enzyme 741988 7.1.1.3 W147L the mutation does not affect the in vivo activity 714141 7.1.1.3 W156A the mutant of subunit III shows 70% activity compared to the wild type enzyme 741988 7.1.1.3 W280L 67% activity compared to the wild type enzyme 714141 7.1.1.3 W282F the mutation does not affect the in vivo activity 714141 7.1.1.3 W331L 19% activity compared to the wild type enzyme 714141 7.1.1.3 Y173F the mutant possesses 91% copper and 108% cytochrome o compared to the wild type enzyme -, 715399 7.1.1.3 Y288F the mutations specifically eliminates the CuB center from the oxidase complex 715399 7.1.1.3 Y288L 0.3% activity compared to the wild type enzyme 714141 7.1.1.3 Y61F the mutation does not affect the in vivo activity -, 714141