Ultrafast Dynamics and Vibrational Relaxation in Six-Coordinate Heme Proteins Revealed by Femtosecond Stimulated Raman Spectroscopy

Carino Ferrante (1) , Giovanni Batignani , Emanuele Pontecorvo (2) , Linda Montemiglio , Marten H. Vos (3) , Tullio Scopigno

1 CNISM, Dipartimento di Fisica,
2 ESRF - European Synchrotron Radiation Facility
3 LOB - Laboratoire d'Optique et Biosciences

Identifying the structural rearrangement and the active sites in photo-induced reactions is a fundamental challenge to understand from a microscopic perspective the underlying dynamics ruling the functional mechanisms of heme proteins. Here, femtosecond stimulated Raman spectroscopy is used to follow the ultrafast evolution of two 1 six-coordinate heme proteins. By exploiting the sensitivity of Raman spectra to the structural conguration, we investigate the eects of photolysis and binding of amino acid residues in cytochrome c and neuroglobin. Comparing the system response for different time delays and Raman pump resonances, we show how details of atomic motions and energy redistribution can be unveiled.

Domaines: Biochimie, Biologie Moléculaire; Biophysique

Carino Ferrante, Giovanni Batignani, Emanuele Pontecorvo, Linda Montemiglio, Marten H. Vos, et al.. Ultrafast Dynamics and Vibrational Relaxation in Six-Coordinate Heme Proteins Revealed by Femtosecond Stimulated Raman Spectroscopy. Journal of the American Chemical Society, 2020, 142 (5), pp.2285-2292. ⟨10.1021/jacs.9b10560⟩. ⟨hal-02469082⟩