Direct observation of ligand transfer and bond formation in cytochrome c oxidase by using mid-infrared chirped-pulse upconversion.

ABSTRACT: We have implemented the recently demonstrated technique of chirped-pulse upconversion of midinfrared femtosecond pulses into the visible in a visible pump-midinfrared probe experiment for high-resolution, high-sensitivity measurements over a broad spectral range. We have succeeded in time-resolving the CO ligand transfer process from the heme Fe to the neighboring Cu(B) atom in the bimetallic active site of mammalian cytochrome c oxidase, which was known to proceed in <1 ps, using the full CO vibrational signature of Fe-CO bond breaking and Cu(B)-CO bond formation. Our differential transmission results show a delayed onset of the appearance of the Cu(B)-bound species (200 fs), followed by a 450-fs exponential rise. Trajectories calculated by using molecular-dynamics simulations with a Morse potential for the Cu(B)-C interaction display a similar behavior. Both experimental and calculated data strongly suggest a ballistic contribution to the transfer process.

SUBMITTER: Treuffet J 

PROVIDER: S-EPMC2000433 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature