Ultrafast tryptophan-to-heme electron transfer in myoglobins revealed by UV 2D spectroscopy

Tryptophan is commonly used to study protein structure and dynamics, such as protein folding, as a donor in fluorescence resonant energy transfer (FRET) studies. By using ultra-broadband ultrafast two-dimensional (2D) spectroscopy in the ultraviolet (UV) and transient absorption in the visible range...

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Published in:	Science (American Association for the Advancement of Science) Vol. 339; no. 6127; p. 1586
Main Authors:	Consani, Cristina, Auböck, Gerald, van Mourik, Frank, Chergui, Majed
Format:	Journal Article
Language:	English
Published:	United States 29.03.2013
Subjects:	Animals Electron Transport Fluorescence Resonance Energy Transfer Heme - chemistry Horses Myoglobin - chemistry Protein Structure, Secondary Spectrophotometry, Ultraviolet - methods Tryptophan - chemistry
ISSN:	1095-9203, 1095-9203
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Abstract	Tryptophan is commonly used to study protein structure and dynamics, such as protein folding, as a donor in fluorescence resonant energy transfer (FRET) studies. By using ultra-broadband ultrafast two-dimensional (2D) spectroscopy in the ultraviolet (UV) and transient absorption in the visible range, we have disentangled the excited state decay pathways of the tryptophan amino acid residues in ferric myoglobins (MbCN and metMb). Whereas the more distant tryptophan (Trp(7)) relaxes by energy transfer to the heme, Trp(14) excitation predominantly decays by electron transfer to the heme. The excited Trp(14)→heme electron transfer occurs in <40 picoseconds with a quantum yield of more than 60%, over an edge-to-edge distance below ~10 angstroms, outcompeting the FRET process. Our results raise the question of whether such electron transfer pathways occur in a larger class of proteins.
AbstractList	Tryptophan is commonly used to study protein structure and dynamics, such as protein folding, as a donor in fluorescence resonant energy transfer (FRET) studies. By using ultra-broadband ultrafast two-dimensional (2D) spectroscopy in the ultraviolet (UV) and transient absorption in the visible range, we have disentangled the excited state decay pathways of the tryptophan amino acid residues in ferric myoglobins (MbCN and metMb). Whereas the more distant tryptophan (Trp(7)) relaxes by energy transfer to the heme, Trp(14) excitation predominantly decays by electron transfer to the heme. The excited Trp(14)→heme electron transfer occurs in <40 picoseconds with a quantum yield of more than 60%, over an edge-to-edge distance below ~10 angstroms, outcompeting the FRET process. Our results raise the question of whether such electron transfer pathways occur in a larger class of proteins.Tryptophan is commonly used to study protein structure and dynamics, such as protein folding, as a donor in fluorescence resonant energy transfer (FRET) studies. By using ultra-broadband ultrafast two-dimensional (2D) spectroscopy in the ultraviolet (UV) and transient absorption in the visible range, we have disentangled the excited state decay pathways of the tryptophan amino acid residues in ferric myoglobins (MbCN and metMb). Whereas the more distant tryptophan (Trp(7)) relaxes by energy transfer to the heme, Trp(14) excitation predominantly decays by electron transfer to the heme. The excited Trp(14)→heme electron transfer occurs in <40 picoseconds with a quantum yield of more than 60%, over an edge-to-edge distance below ~10 angstroms, outcompeting the FRET process. Our results raise the question of whether such electron transfer pathways occur in a larger class of proteins. Tryptophan is commonly used to study protein structure and dynamics, such as protein folding, as a donor in fluorescence resonant energy transfer (FRET) studies. By using ultra-broadband ultrafast two-dimensional (2D) spectroscopy in the ultraviolet (UV) and transient absorption in the visible range, we have disentangled the excited state decay pathways of the tryptophan amino acid residues in ferric myoglobins (MbCN and metMb). Whereas the more distant tryptophan (Trp(7)) relaxes by energy transfer to the heme, Trp(14) excitation predominantly decays by electron transfer to the heme. The excited Trp(14)→heme electron transfer occurs in <40 picoseconds with a quantum yield of more than 60%, over an edge-to-edge distance below ~10 angstroms, outcompeting the FRET process. Our results raise the question of whether such electron transfer pathways occur in a larger class of proteins.
Author	van Mourik, Frank Auböck, Gerald Chergui, Majed Consani, Cristina
Author_xml	– sequence: 1 givenname: Cristina surname: Consani fullname: Consani, Cristina organization: Laboratory of Ultrafast Spectroscopy, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland – sequence: 2 givenname: Gerald surname: Auböck fullname: Auböck, Gerald – sequence: 3 givenname: Frank surname: van Mourik fullname: van Mourik, Frank – sequence: 4 givenname: Majed surname: Chergui fullname: Chergui, Majed
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SubjectTerms	Animals Electron Transport Fluorescence Resonance Energy Transfer Heme - chemistry Horses Myoglobin - chemistry Protein Structure, Secondary Spectrophotometry, Ultraviolet - methods Tryptophan - chemistry
Title	Ultrafast tryptophan-to-heme electron transfer in myoglobins revealed by UV 2D spectroscopy
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