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dc.contributor.author
Wagner, Jeremiah R.
dc.contributor.author
Zhang, Junrui
dc.contributor.author
Von Stetten, David
dc.contributor.author
Günther, Mina
dc.contributor.author
Murgida, Daniel Horacio
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dc.contributor.author
Mroginski, Maria Andrea
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Walker, Joseph M.
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Forest, Katrina T.
dc.contributor.author
Hildebrandt, Peter
dc.contributor.author
Vierstra, Richard D.
dc.date.available
2019-09-16T21:27:44Z
dc.date.issued
2008-05
dc.identifier.citation
Wagner, Jeremiah R.; Zhang, Junrui; Von Stetten, David; Günther, Mina; Murgida, Daniel Horacio; et al.; Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 283; 18; 5-2008; 12212-12226
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/83697
dc.description.abstract
The ability of phytochromes (Phy) to act as photointerconvertible light switches in plants and microorganisms depends on key interactions between the bilin chromophore and the apoprotein that promote bilin attachment and photointerconversion between the spectrally distinct red light-absorbing Pr conformer and far red light-absorbing Pfr conformer. Using structurally guided site-directed mutagenesis combined with several spectroscopic methods, we examined the roles of conserved amino acids within the bilin-binding domain of Deinococcus radiodurans bacteriophytochrome with respect to chromophore ligation and Pr/Pfr photoconversion. Incorporation of biliverdin IXα (BV), its structure in the Pr state, and its ability to photoisomerize to the first photocycle intermediate are insensitive to most single mutations, implying that these properties are robust with respect to small structural/electrostatic alterations in the binding pocket. In contrast, photoconversion to Pfr is highly sensitive to the chromophore environment. Many of the variants form spectrally bleached Meta-type intermediates in red light that do not relax to Pfr. Particularly important are Asp-207 and His-260, which are invariant within the Phy superfamily and participate in a unique hydrogen bond matrix involving the A, B, and C pyrrole ring nitrogens of BV and their associated pyrrole water. Resonance Raman spectroscopy demonstrates that substitutions of these residues disrupt the Pr to Pfr protonation cycle of BV with the chromophore locked in a deprotonated Meta-Rc-like photoconversion intermediate after red light irradiation. Collectively, the data show that a number of contacts contribute to the unique photochromicity of Phy-type photoreceptors. These include residues that fix the bilin in the pocket, coordinate the pyrrole water, and possibly promote the proton exchange cycle during photoconversion.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Phytochromes
dc.subject
Photoreceptors
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Ft-Raman
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Dft Calculations
dc.subject.classification
Físico-Química, Ciencia de los Polímeros, Electroquímica
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dc.subject.classification
Ciencias Químicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-06-11T18:14:22Z
dc.journal.volume
283
dc.journal.number
18
dc.journal.pagination
12212-12226
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Bethesda
dc.description.fil
Fil: Wagner, Jeremiah R.. Beloit College; Estados Unidos. University of Wisconsin; Estados Unidos
dc.description.fil
Fil: Zhang, Junrui. University of Wisconsin; Estados Unidos
dc.description.fil
Fil: Von Stetten, David. Technishe Universitat Berlin; Alemania
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Fil: Günther, Mina. Technishe Universitat Berlin; Alemania
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Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Technishe Universitat Berlin; Alemania
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Fil: Mroginski, Maria Andrea. Technishe Universitat Berlin; Alemania
dc.description.fil
Fil: Walker, Joseph M.. University of Wisconsin; Estados Unidos
dc.description.fil
Fil: Forest, Katrina T.. University of Wisconsin; Estados Unidos
dc.description.fil
Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania
dc.description.fil
Fil: Vierstra, Richard D.. University of Wisconsin; Estados Unidos
dc.journal.title
Journal of Biological Chemistry (online)
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M709355200
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/283/18/12212
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