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dc.contributor.author
Rose, Samuel L.
dc.contributor.author
Ferroni, Felix Martín
dc.contributor.author
Horrell, Sam
dc.contributor.author
Brondino, Carlos Dante
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Eady, Robert R.
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Jaho, Sofia
dc.contributor.author
Hough, Michael A.
dc.contributor.author
Owen, Robin L.
dc.contributor.author
Antonyuk, Svetlana V.
dc.contributor.author
Hasnain, S. Samar
dc.date.available
2024-08-15T13:27:02Z
dc.date.issued
2024-09
dc.identifier.citation
Rose, Samuel L.; Ferroni, Felix Martín; Horrell, Sam; Brondino, Carlos Dante; Eady, Robert R.; et al.; Spectroscopically Validated pH-dependent MSOX Movies Provide Detailed Mechanism of Copper Nitrite Reductases; Academic Press Ltd - Elsevier Science Ltd; Journal of Molecular Biology; 436; 18; 9-2024; 1-17
dc.identifier.issn
0022-2836
dc.identifier.uri
http://hdl.handle.net/11336/242585
dc.description.abstract
Copper nitrite reductases (CuNiRs) exhibit a strong pH dependence of their catalytic activity. Structural movies can be obtained by serially recording multiple structures (frames) from the same spot of a crystal using the MSOX serial crystallography approach. This method has been combined with on-line single crystal optical spectroscopy to capture the pH-dependent structural changes that accompany during turnover of CuNiRs from two Rhizobia species. The structural movies, initiated by the redox activation of a type-1 copper site (T1Cu) via X-ray generated photoelectrons, have been obtained for the substrate-free and substrate-bound states at low (high enzymatic activity) and high (low enzymatic activity) pH. At low pH, formation of the product nitric oxide (NO) is complete at the catalytic type-2 copper site (T2Cu) after a dose of 3 MGy (frame 5) with full bleaching of the T1Cu ligand-to-metal charge transfer (LMCT) 455 nm band (S(σ)Cys → T1Cu2+) which in itself indicates the electronic route of proton-coupled electron transfer (PCET) from T1Cu to T2Cu. In contrast at high pH, the changes in optical spectra are relatively small and the formation of NO is only observed in later frames (frame 15 in Br2DNiR, 10 MGy), consistent with the loss of PCET required for catalysis. This is accompanied by decarboxylation of the catalytic AspCAT residue, with CO2 trapped in the catalytic pocket.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Academic Press Ltd - Elsevier Science Ltd
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
DENITRIFICATION
dc.subject
CATALYSIS
dc.subject
PROTON TRANSFER
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ELECTRON TRANSFER
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SUBSTRATE UTILISATION
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Biofísica
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Spectroscopically Validated pH-dependent MSOX Movies Provide Detailed Mechanism of Copper Nitrite Reductases
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2024-08-12T13:14:07Z
dc.journal.volume
436
dc.journal.number
18
dc.journal.pagination
1-17
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Rose, Samuel L.. University Of Liverpool. Faculty Of Health And Life Sciences. Institute Of Integrative Biology. Barkla X -ray Laboratory Of Biophysics.; Reino Unido
dc.description.fil
Fil: Ferroni, Felix Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. University Of Liverpool. Faculty Of Health And Life Sciences. Institute Of Integrative Biology. Barkla X -ray Laboratory Of Biophysics.; Reino Unido
dc.description.fil
Fil: Horrell, Sam. Diamond Lightsource; Reino Unido
dc.description.fil
Fil: Brondino, Carlos Dante. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina
dc.description.fil
Fil: Eady, Robert R.. University Of Liverpool. Faculty Of Health And Life Sciences. Institute Of Integrative Biology. Barkla X -ray Laboratory Of Biophysics.; Reino Unido
dc.description.fil
Fil: Jaho, Sofia. Diamond Lightsource; Reino Unido
dc.description.fil
Fil: Hough, Michael A.. Diamond Lightsource; Reino Unido
dc.description.fil
Fil: Owen, Robin L.. Diamond Lightsource; Reino Unido
dc.description.fil
Fil: Antonyuk, Svetlana V.. University Of Liverpool. Faculty Of Health And Life Sciences. Institute Of Integrative Biology. Barkla X -ray Laboratory Of Biophysics.; Reino Unido
dc.description.fil
Fil: Hasnain, S. Samar. University Of Liverpool. Faculty Of Health And Life Sciences. Institute Of Integrative Biology. Barkla X -ray Laboratory Of Biophysics.; Reino Unido
dc.journal.title
Journal of Molecular Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0022283624003152
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/j.jmb.2024.168706
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