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Direct observation of two-channel photodissociation of carbon monoxide from the hemoglobin subunits

Author

Listed:
  • Sergei V. Lepeshkevich

    (National Academy of Sciences of Belarus)

  • Igor V. Sazanovich

    (STFC Rutherford Appleton Laboratory)

  • Marina V. Parkhats

    (National Academy of Sciences of Belarus)

  • Syargey N. Gilevich

    (National Academy of Sciences of Belarus)

  • Aliaksei V. Yantsevich

    (National Academy of Sciences of Belarus)

  • Julia A. Weinstein

    (Brook Hill)

  • Michael Towrie

    (STFC Rutherford Appleton Laboratory)

  • Boris M. Dzhagarov

    (National Academy of Sciences of Belarus)

Abstract

Determining dynamics of bond breaking between carbon monoxide (CO) and heme proteins is essential to understand the interplay between protein function and dynamics, which is one of the fundamental challenges of physical biology. There is an ongoing debate about the mechanism of CO photodissociation from the heme iron. Here we use picosecond to millisecond transient mid-infrared spectroscopy to determine the dynamics of CO photodissociation from the isolated human hemoglobin chains. We find that the breaking of the Fe–CO bond is not a single-step process as is commonly accepted, but rather at least a two-step process, which includes both the known prompt sub-50-fs CO dissociation event and the additional slower, ~15 ps CO dissociation process discovered in this study. These results offer the direct experimental proof of the CO photodissociation mechanism containing several dissociative states.

Suggested Citation

  • Sergei V. Lepeshkevich & Igor V. Sazanovich & Marina V. Parkhats & Syargey N. Gilevich & Aliaksei V. Yantsevich & Julia A. Weinstein & Michael Towrie & Boris M. Dzhagarov, 2025. "Direct observation of two-channel photodissociation of carbon monoxide from the hemoglobin subunits," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-63092-z
    DOI: 10.1038/s41467-025-63092-z
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    References listed on IDEAS

    as
    1. Konstantin Falahati & Hiroyuki Tamura & Irene Burghardt & Miquel Huix-Rotllant, 2018. "Ultrafast carbon monoxide photolysis and heme spin-crossover in myoglobin via nonadiabatic quantum dynamics," Nature Communications, Nature, vol. 9(1), pages 1-8, December.
    2. Matteo Levantino & Giorgio Schirò & Henrik Till Lemke & Grazia Cottone & James Michael Glownia & Diling Zhu & Mathieu Chollet & Hyotcherl Ihee & Antonio Cupane & Marco Cammarata, 2015. "Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser," Nature Communications, Nature, vol. 6(1), pages 1-6, November.
    3. Marco E. Reinhard & Michael W. Mara & Thomas Kroll & Hyeongtaek Lim & Ryan G. Hadt & Roberto Alonso-Mori & Matthieu Chollet & James M. Glownia & Silke Nelson & Dimosthenis Sokaras & Kristjan Kunnus & , 2021. "Short-lived metal-centered excited state initiates iron-methionine photodissociation in ferrous cytochrome c," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
    4. Dominik Kinschel & Camila Bacellar & Oliviero Cannelli & Boris Sorokin & Tetsuo Katayama & Giulia F. Mancini & Jérémy R. Rouxel & Yuki Obara & Junichi Nishitani & Hironori Ito & Terumasa Ito & Naoya K, 2020. "Femtosecond X-ray emission study of the spin cross-over dynamics in haem proteins," Nature Communications, Nature, vol. 11(1), pages 1-8, December.
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