Time-resolved OH-->EH transition of the aberrant ba3 oxidase from Thermus thermophilus.
The kinetics of single-electron injection into the oxidized nonrelaxed state (OH --> EH transition) of the aberrant ba3 cytochrome oxidase from Thermus thermophilus, noted for its lowered efficiency of proton pumping, was investigated by time-resolved optical spectroscopy. Two main phases of intraprotein electron transfer were resolved. The first component (tau approximately 17 mus) reflects oxidation of CuA and reduction of the heme groups (low-spin heme b and high-spin heme a3 in a ratio close to 50:50). The subsequent component (tau 420 mus) includes reoxidation of both hemes by CuB. This is in significant contrast to the OH--> EH transition of the aa3-type cytochrome oxidase from Paracoccus denitrificans, where the fastest phase is exclusively due to transient reduction of the low-spin heme a, without electron equilibration with the binuclear center. On the other hand, the one-electron reduction of the relaxed O state in ba3 oxidase was similar to that in aa3 oxidase and only included rapid electron transfer from CuA to the low-spin heme b. This indicates a functional difference between the relaxed O and the pulsed OH forms also in the ba3 oxidase from T. thermophilus.
Siletsky
Sergey A
SA
Department of Molecular Energetics of Microorganisms, Lomonosov Moscow State University, Moscow, Russian Federation.
Belevich
Ilya
I
Wikström
Mårten
M
Soulimane
Tewfik
T
Verkhovsky
Michael I
MI
D002384:Catalysis; D003573:Cytochrome b Group / Q000737:chemistry* / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism*; D006418:Heme / Q000737:chemistry*; D006878:Hydroxides / Q000737:chemistry*; D007700:Kinetics; D016963:Thermus thermophilus / Q000201:enzymology*
D003573:Cytochrome b Group; D006878:Hydroxides; D006418:Heme; C031356:hydroxide ion; C058557:cytochrome ba3; D003576:Electron Transport Complex IV