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  Glutamine rotamers in BLUF photoreceptors: a mechanistic reappraisal

Udvarhelyi, A., & Domratcheva, T. (2013). Glutamine rotamers in BLUF photoreceptors: a mechanistic reappraisal. Journal of Physical Chemistry B, 117(10), 2888-2897. doi:10.1021/jp400437x.

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Udvarhelyi, Anikó1, Author              
Domratcheva, Tatiana1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: The blue light using FAD (BLUF) photosensory protein domain is activated by a unique photoreaction that results in a hydrogen-bond rearrangement around the flavin chromophore. The chemical structure of the hydrogen bond switch is a long-standing debate: The two main hypotheses postulate rotation as opposed to tautomerization of a conserved glutamine residue. Attempts to resolve the debate were inconclusive so far, despite numerous experimental and computational studies. Here we propose physical criteria for the dark and light state structures as well as for the light-activation process to evaluate existing models of BLUF using quantum-chemical calculations. The glutamine rotamer assignment of the crystal structure with the pdb code 1YRX does not satisfy our criteria because after equilibrating the intermolecular forces the glutamine rotamer in 1YRX is incompatible with the experimental density. We identified the root of the mechanistic controversy in the incorrect glutamine rotamer assignment of 1YRX . Furthermore, we show that the glutamine side chain may rotate without light activation in the BLUF dark state. Finally, we demonstrate that the tautomerized glutamine is consistent with our criteria and observations of the BLUF light state

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Language(s): eng - English
 Dates: 2013-01-142013-02-192013-02-192013-03-14
 Publication Status: Published in print
 Pages: 10
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jp400437x
Other: 7893
 Degree: -

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Title: Journal of Physical Chemistry B
Source Genre: Journal
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Pages: - Volume / Issue: 117 (10) Sequence Number: - Start / End Page: 2888 - 2897 Identifier: ISSN: 1520-6106
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000293370