Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein

Pande, K

doi:10.11577/1573793

Title: Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein

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Authors:

Pande, K

CXIDB

Publication Date:: Tue Nov 05 23:00:00 EST 2019

Other Number(s):: CXIDB ID 118

DOE Contract Number:: AC02-05CH11231

Research Org.:: Coherent X-ray Imaging Data Bank (Lawrence Berkeley National Laboratory); UWM, LBNL, SLAC, CFEL, U Chicago

Sponsoring Org.:: UWM, LBNL, SLAC, CFEL, U Chicago

Subject:: CXI; LCLS; Photoactive yellow protein (PYP); Serial Femtosecond Crystallography; X-ray Free-electorn Lasers; XFEL

OSTI Identifier:: 1573793

DOI:: https://doi.org/10.11577/1573793

Citation Formats


                    Pande, K. Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein.  United States: N. p., 2019. 
        Web.  doi:10.11577/1573793.

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                    Pande, K. Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein.  United States.  doi:https://doi.org/10.11577/1573793

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                    Pande, K. 2019.  
"Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein".  United States.  doi:https://doi.org/10.11577/1573793.  https://www.osti.gov/servlets/purl/1573793. Pub date:Tue Nov 05 23:00:00 EST 2019

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@article{osti_1573793,

  title        = {Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein},

  author       = {Pande, K},

  abstractNote = {},

  doi          = {10.11577/1573793},

  journal      = {},

  number       = ,

  volume       = ,

  place        = {United States},

  year         = {Tue Nov 05 23:00:00 EST 2019},

  month        = {Tue Nov 05 23:00:00 EST 2019}

}

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DOI: https://doi.org/10.11577/1573793

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A variety of organisms have evolved mechanisms to detect and respond to light, in which the response is mediated by protein structural changes following photon absorption. The initial step is often the photo-isomerization of a conjugated chromophore. Furthermore, isomerization occurs on ultrafast timescales and is substantially influenced by the chromophore environment. Here we identify structural changes associated with the earliest steps in the trans to cis isomerization of the chromophore in photoactive yellow protein. Femtosecond, hard X-ray pulses emitted by the Linac Coherent Light Source were used to conduct time-resolved serial femtosecond crystallography on PYP microcrystals over the time rangemore »« less
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Trans-to-cis isomerization, the key reaction in photoactive proteins, usually cannot occur through the standard one-bond-flip mechanism. Owing to spatial constraints imposed by a protein environment, isomerization probably proceeds through a volume-conserving mechanism in which highly choreographed atomic motions are expected, the details of which have not yet been observed directly. Here we employ time-resolved X-ray crystallography to visualize structurally the isomerization of the p-coumaric acid chromophore in photoactive yellow protein with a time resolution of 100 ps and a spatial resolution of 1.6 Å. The structure of the earliest intermediate (I_T) resembles a highly strained transition state in which themore »« less
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