Surprising intrinsic photostability of the disulfide bridge common in proteins

Anne Boutrup Stephansen; Rasmus Yding Brogaard; Thomas Scheby Kuhlman; Liv Bærenholdt Klein; Jørn Bolstad Christensen; Theis Ivan Sølling

doi:10.1021/ja310540a

Surprising intrinsic photostability of the disulfide bridge common in proteins

Anne Boutrup Stephansen, Rasmus Yding Brogaard, Thomas Scheby Kuhlman, Liv Bærenholdt Klein, Jørn Bolstad Christensen, Theis Ivan Sølling

Department of Chemistry

14 Citations (Scopus)

Abstract

For a molecule to survive evolution and to become a key building block in nature, photochemical stability is essential. The photolytically weak S-S bond does not immediately seem to possess that ability. We mapped the real-time motion of the two sulfur radicals that result from disulfide photolysis on the femtosecond time scale and found the reason for the existence of the S-S bridge as a natural building block in folded structures. The sulfur atoms will indeed move apart on the excited state but only to oscillate around the S-S center of mass. At long S-S distances, there is a strong coupling to the ground state, and the oscillatory motion enables the molecules to continuously revisit that particular region of the potential energy surface. When a structural feature such as a ring prevents the sulfur radicals from flying apart and thus assures a sufficient residence time in the active region of the potential energy surface, the electronic energy is converted into less harmful vibrational energy, thereby restoring the S-S bond in the ground state.

Original language	English
Journal	Journal of the American Chemical Society
Volume	134
Issue number	50
Pages (from-to)	20279-20281
Number of pages	3
ISSN	0002-7863
DOIs	https://doi.org/10.1021/ja310540a
Publication status	Published - 19 Dec 2012

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title = "Surprising intrinsic photostability of the disulfide bridge common in proteins",

abstract = "For a molecule to survive evolution and to become a key building block in nature, photochemical stability is essential. The photolytically weak S-S bond does not immediately seem to possess that ability. We mapped the real-time motion of the two sulfur radicals that result from disulfide photolysis on the femtosecond time scale and found the reason for the existence of the S-S bridge as a natural building block in folded structures. The sulfur atoms will indeed move apart on the excited state but only to oscillate around the S-S center of mass. At long S-S distances, there is a strong coupling to the ground state, and the oscillatory motion enables the molecules to continuously revisit that particular region of the potential energy surface. When a structural feature such as a ring prevents the sulfur radicals from flying apart and thus assures a sufficient residence time in the active region of the potential energy surface, the electronic energy is converted into less harmful vibrational energy, thereby restoring the S-S bond in the ground state.",

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T1 - Surprising intrinsic photostability of the disulfide bridge common in proteins

AU - Stephansen, Anne Boutrup

AU - Brogaard, Rasmus Yding

AU - Kuhlman, Thomas Scheby

AU - Klein, Liv Bærenholdt

AU - Christensen, Jørn Bolstad

AU - Sølling, Theis Ivan

PY - 2012/12/19

Y1 - 2012/12/19

N2 - For a molecule to survive evolution and to become a key building block in nature, photochemical stability is essential. The photolytically weak S-S bond does not immediately seem to possess that ability. We mapped the real-time motion of the two sulfur radicals that result from disulfide photolysis on the femtosecond time scale and found the reason for the existence of the S-S bridge as a natural building block in folded structures. The sulfur atoms will indeed move apart on the excited state but only to oscillate around the S-S center of mass. At long S-S distances, there is a strong coupling to the ground state, and the oscillatory motion enables the molecules to continuously revisit that particular region of the potential energy surface. When a structural feature such as a ring prevents the sulfur radicals from flying apart and thus assures a sufficient residence time in the active region of the potential energy surface, the electronic energy is converted into less harmful vibrational energy, thereby restoring the S-S bond in the ground state.

AB - For a molecule to survive evolution and to become a key building block in nature, photochemical stability is essential. The photolytically weak S-S bond does not immediately seem to possess that ability. We mapped the real-time motion of the two sulfur radicals that result from disulfide photolysis on the femtosecond time scale and found the reason for the existence of the S-S bridge as a natural building block in folded structures. The sulfur atoms will indeed move apart on the excited state but only to oscillate around the S-S center of mass. At long S-S distances, there is a strong coupling to the ground state, and the oscillatory motion enables the molecules to continuously revisit that particular region of the potential energy surface. When a structural feature such as a ring prevents the sulfur radicals from flying apart and thus assures a sufficient residence time in the active region of the potential energy surface, the electronic energy is converted into less harmful vibrational energy, thereby restoring the S-S bond in the ground state.

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DO - 10.1021/ja310540a

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

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Surprising intrinsic photostability of the disulfide bridge common in proteins

Abstract

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