Document Detail

Vibrational Assignment of the Ultrafast Infrared Spectrum of the Photoactivatable Flavoprotein AppA.
MedLine Citation:
PMID:  22871066     Owner:  NLM     Status:  Publisher    
The blue light using flavin (BLUF) domain proteins, such as the transcriptional antirepressor AppA, are a novel class of photosensors that bind flavin noncovalently in order to sense and respond to high intensity blue (450 nm) light. Importantly, the non-covalently bound flavin chromophore is unable to undergo large scale structural change upon light absorption, and thus there is significant interest in understanding how the BLUF protein matrix senses and responds to flavin photoexcitation. Light absorption is proposed to result in alterations in the hydrogen bonding network that surrounds the flavin chromophore on an ultrafast time scale, and the structural changes caused by photoexcitation are being probed by vibrational spectroscopy. Here we report ultrafast time resolved infrared spectra of the AppA BLUF domain (AppABLUF) reconstituted with isotopes of FAD, specifically [U-13C17]-FAD, [xylene-13C8]-FAD, [U-15N4]-FAD and [4-18O1]-FAD both in solution and bound to AppABLUF. This allows for unambiguous assignment of ground and excited state modes arising directly from the flavin. Studies of model compounds and DFT calculations of the ground state vibrational spectra reveal the sensitivity of these modes to their environment, indicating they can be used as probes of structural dynamics.
Allison Laura Haigney; Andras Lukacs; Richard James Brust; Rui-Kun Zhao; Michael Towrie; Gregory M Greetham; Ian P Clark; Boris Illarionov; Adelbert Bacher; Ryu-Ryun Kim; Markus Fischer; Stephen Roy Meech; Peter J Tonge
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-8-7
Journal Detail:
Title:  The journal of physical chemistry. B     Volume:  -     ISSN:  1520-5207     ISO Abbreviation:  J Phys Chem B     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-8-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101157530     Medline TA:  J Phys Chem B     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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