Literature DB >> 17523627

Picosecond protein response to the chromophore isomerization of photoactive yellow protein: selective observation of tyrosine and tryptophan residues by time-resolved ultraviolet resonance Raman spectroscopy.

Misao Mizuno, Norio Hamada, Fumio Tokunaga, Yasuhisa Mizutani.   

Abstract

Picosecond time-resolved ultraviolet resonance Raman (UVRR) spectra of photoactive yellow protein (PYP) were measured. UVRR bands attributed to the vibration of tyrosine and tryptophan residues showed a spectral change upon photoreaction. It was found that the hydrogen-bond strength between the chromophore and Y42 increases in the pG* state. The ultrafast change in the tryptophan band revealed that a photoinduced structural change of the chromophore had propagated to the W119 region, located 12 A from the chromophore, within picoseconds.

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Year:  2007        PMID: 17523627     DOI: 10.1021/jp072939d

Source DB:  PubMed          Journal:  J Phys Chem B        ISSN: 1520-5207            Impact factor:   2.991


  3 in total

1.  Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy.

Authors:  Ignacio López-Peña; Brian S Leigh; Diana E Schlamadinger; Judy E Kim
Journal:  Biochemistry       Date:  2015-07-29       Impact factor: 3.162

Review 2.  Role of atomic contacts in vibrational energy transfer in myoglobin.

Authors:  Misao Mizuno; Yasuhisa Mizutani
Journal:  Biophys Rev       Date:  2020-03-23

3.  Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.

Authors:  Sang Jin Lee; Youngmin Kim; Tae Wu Kim; Cheolhee Yang; Kamatchi Thamilselvan; Hyeongseop Jeong; Jaekyung Hyun; Hyotcherl Ihee
Journal:  Cell Rep Phys Sci       Date:  2021-07-22
  3 in total

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