Proteins in Action: Femtosecond to Millisecond Structural Dynamics of a Photoactive Flavoprotein
Open Access
- 22 October 2013
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 135 (43), 16168-16174
- https://doi.org/10.1021/ja407265p
Abstract
Living systems are fundamentally dependent on the ability of proteins to respond to external stimuli. The mechanism, the underlying structural dynamics, and the time scales for regulation of this response are central questions in biochemistry. Here we probe the structural dynamics of the BLUF domain found in several photoactive flavoproteins, which is responsible for light activated functions as diverse as phototaxis and gene regulation. Measurements have been made over 10 decades of time (from 100 fs to 1 ms) using transient vibrational spectroscopy. Chromophore (flavin ring) localized dynamics occur on the pico- to nanosecond time scale, while subsequent protein structural reorganization is observed over microseconds. Multiple time scales are observed for the dynamics associated with different vibrations of the protein, suggesting an underlying hierarchical relaxation pathway. Structural evolution in residues directly H-bonded to the chromophore takes place more slowly than changes in more remote residues. However, a point mutation which suppresses biological function is shown to ‘short circuit’ this structural relaxation pathway, suppressing the changes which occur further away from the chromophore while accelerating dynamics close to it.Keywords
This publication has 44 references indexed in Scilit:
- Watching a signaling protein function in real time via 100-ps time-resolved Laue crystallographyProceedings of the National Academy of Sciences of the United States of America, 2012
- Vibrational Assignment of the Ultrafast Infrared Spectrum of the Photoactivatable Flavoprotein AppAThe Journal of Physical Chemistry B, 2012
- Direct Observation of Cooperative Protein Structural Dynamics of Homodimeric Hemoglobin from 100 ps to 10 ms with Pump–Probe X-ray Solution ScatteringJournal of the American Chemical Society, 2012
- N-α-Benzoyl-N5-(2-Chloro-1-Iminoethyl)-l-Ornithine Amide, a Protein Arginine Deiminase Inhibitor, Reduces the Severity of Murine Collagen-Induced ArthritisPublished by The American Association of Immunologists ,2011
- Light Modulation of Cellular cAMP by a Small Bacterial Photoactivated Adenylyl Cyclase, bPAC, of the Soil Bacterium BeggiatoaPublished by Elsevier BV ,2011
- Protein structural dynamics in solution unveiled via 100-ps time-resolved x-ray scatteringProceedings of the National Academy of Sciences of the United States of America, 2010
- Analysis of photoinduced electron transfer in AppAJournal of Photochemistry and Photobiology A: Chemistry, 2009
- Spectroscopic Studies of the AppA BLUF Domain from Rhodobacter sphaeroides: Addressing Movement of Tryptophan 104 in the Signaling StateBiochemistry, 2009
- Molecular Models Predict Light-Induced Glutamine Tautomerization in BLUF PhotoreceptorsBiophysical Journal, 2008
- The Critical Role of a Hydrogen Bond between Gln63 and Trp104 in the Blue-Light Sensing BLUF Domain That Controls AppA ActivityJournal of Molecular Biology, 2007