Time-resolved OH-->EH transition of the aberrant ba3 oxidase from Thermus thermophilus

Biochim Biophys Acta. 2009 Mar;1787(3):201-5. doi: 10.1016/j.bbabio.2008.12.020.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Cytochrome b Group / chemistry*
  • Cytochrome b Group / metabolism*
  • Electron Transport Complex IV / chemistry*
  • Electron Transport Complex IV / metabolism*
  • Heme / chemistry*
  • Hydroxides / chemistry*
  • Kinetics
  • Thermus thermophilus / enzymology*

Substances

  • Cytochrome b Group
  • Hydroxides
  • Heme
  • hydroxide ion
  • cytochrome ba3
  • Electron Transport Complex IV