Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering

Yunbeom Lee, Jong Goo Kim, Sang Jin Lee, Srinivasan Muniyappan, Tae Wu Kim, Hosung Ki, Hanui Kim, Junbeom Jo, So Ri Yun, Hyosub Lee, Kyung Won Lee, Seong Ok Kim, Marco Cammarata and Hyotcherl Ihee ()
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Yunbeom Lee: Korea Advanced Institute of Science and Technology (KAIST)
Jong Goo Kim: Korea Advanced Institute of Science and Technology (KAIST)
Sang Jin Lee: Korea Advanced Institute of Science and Technology (KAIST)
Srinivasan Muniyappan: Korea Advanced Institute of Science and Technology (KAIST)
Tae Wu Kim: Korea Advanced Institute of Science and Technology (KAIST)
Hosung Ki: Korea Advanced Institute of Science and Technology (KAIST)
Hanui Kim: Korea Advanced Institute of Science and Technology (KAIST)
Junbeom Jo: Korea Advanced Institute of Science and Technology (KAIST)
So Ri Yun: Korea Advanced Institute of Science and Technology (KAIST)
Hyosub Lee: Korea Advanced Institute of Science and Technology (KAIST)
Kyung Won Lee: Korea Advanced Institute of Science and Technology (KAIST)
Seong Ok Kim: Korea Advanced Institute of Science and Technology (KAIST)
Marco Cammarata: European Synchrotron Radiation Facility
Hyotcherl Ihee: Korea Advanced Institute of Science and Technology (KAIST)

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract Ultrafast motion of molecules, particularly the coherent motion, has been intensively investigated as a key factor guiding the reaction pathways. Recently, X-ray free-electron lasers (XFELs) have been utilized to elucidate the ultrafast motion of molecules. However, the studies on proteins using XFELs have been typically limited to the crystalline phase, and proteins in solution have rarely been investigated. Here we applied femtosecond time-resolved X-ray solution scattering (fs-TRXSS) and a structure refinement method to visualize the ultrafast motion of a protein. We succeeded in revealing detailed ultrafast structural changes of homodimeric hemoglobin involving the coherent motion. In addition to the motion of the protein itself, the time-dependent change of electron density of the hydration shell was tracked. Besides, the analysis on the fs-TRXSS data of myoglobin allows for observing the effect of the oligomeric state on the ultrafast coherent motion.

Date: 2021
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DOI: 10.1038/s41467-021-23947-7

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