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

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...

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Vydáno v:Nature communications Ročník 16; číslo 1; s. 7746 - 13
Hlavní autoři: Lepeshkevich, Sergei V., Sazanovich, Igor V., Parkhats, Marina V., Gilevich, Syargey N., Yantsevich, Aliaksei V., Weinstein, Julia A., Towrie, Michael, Dzhagarov, Boris M.
Médium: Journal Article
Jazyk:angličtina
Vydáno: London Nature Publishing Group UK 20.08.2025
Nature Publishing Group
Nature Portfolio
Témata:
140/125
631/45
631/45/56
631/45/612/1221
631/57/2272/1590
639/766/747
Binding sites
Carbon monoxide
Carbon Monoxide - chemistry
Carbon Monoxide - metabolism
Chemical bonds
Dynamics
Electric fields
Heme - chemistry
Heme proteins
Hemoglobin
Hemoglobins - chemistry
Hemoglobins - metabolism
Humanities and Social Sciences
Humans
Infrared spectra
Infrared spectroscopy
Iron
Iron - chemistry
Ligands
multidisciplinary
Photodissociation
Protein Subunits - chemistry
Protein Subunits - metabolism
Proteins
Science
Science (multidisciplinary)
Spectrophotometry, Infrared
ISSN:2041-1723, 2041-1723
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Shrnutí: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. Determining dynamics of Fe–CO bond breaking in heme proteins is essential to understand the interplay between protein function and dynamics. Here, the authors report the first experimental proof for the two-step CO photodissociation, involving the previously unknown slower ~15 ps process.
Bibliografie:ObjectType-Article-1
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ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-025-63092-z