Transmembrane charge separation during the ferryl-oxo→ oxidized transition in a nonpumping mutant of cytochrome c oxidase
The N139D mutant of cytochrome c oxidase from Rhodobacter sphaeroides retains full
steady state oxidase activity but completely lacks proton translocation coupled to turnover in
reconstituted liposomes (Pawate, AS, Morgan, J., Namslauer, A., Mills, D., Brzezinski, P.,
Ferguson-Miller, S., and Gennis, RB (2002) Biochemistry 41, 13417–13423). Here, time-
resolved electron transfer and vectorial charge translocation in the ferryl-oxo→ oxidized
transition (transfer of the 4th electron in the catalytic cycle) have been studied with the …
steady state oxidase activity but completely lacks proton translocation coupled to turnover in
reconstituted liposomes (Pawate, AS, Morgan, J., Namslauer, A., Mills, D., Brzezinski, P.,
Ferguson-Miller, S., and Gennis, RB (2002) Biochemistry 41, 13417–13423). Here, time-
resolved electron transfer and vectorial charge translocation in the ferryl-oxo→ oxidized
transition (transfer of the 4th electron in the catalytic cycle) have been studied with the …
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