AbstractExcited electronic states and intraheme relaxation processes in the oxidized and reduced forms of mitochondrial cytochrome c oxidase extracted from a beef heart have been investigated by femtosecond absorption spectroscopy. The spectral and kinetic characteristics of short-lived intermediates have been measured from 80 fs to 20 ps after the photoexcitation. It is found that nonradiative electronic relaxation of the excitation energy in heme a , both in the oxidized (Fe(III) a ) and reduced (Fe(II) a ) forms, occurs successively as three processes, after the end of which heme a is in the ground state with a large store of vibrational energy. The subsequent vibrational relaxation (heme cooling) lasts for several picoseconds. It is found for reduced heme a _3 (Fe(II) a _3) that the electronic relaxation occurs as a result of two successive stages, which changes to vibrational relaxation in the ground state. The mechanism and dynamics of electronic excitation energy conversion in cytochrome c oxidase are analyzed.
Time-Resolved Surface-Enhanced IR-Absorption Spectroscopy of Direct Electron Transfer to Cytochrome c Oxidase from R. sphaeroides
