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© Research
Publication : Proceedings of the National Academy of Sciences of the United States of America

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proceedings of the National Academy of Sciences of the United States of America - 25 Sep 2007

Treuffet J, Kubarych KJ, Lambry JC, Pilet E, Masson JB, Martin JL, Vos MH, Joffre M, Alexandrou A

Link to Pubmed [PMID] – 17895387

Proc. Natl. Acad. Sci. U.S.A. 2007 Oct;104(40):15705-10

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.