Logo do repositório
 
Publicação

Molecular details on multiple cofactor containing redox metalloproteins revealed by infrared and resonance raman spectroscopies

2021-08-02Artigo científico Acesso aberto
Ver registo simples
dc.contributor.authorSilveira, Célia M.
dc.contributor.authorZuccarello, Lidia
dc.contributor.authorBarbosa, Catarina
dc.contributor.authorCaserta, Giorgio
dc.contributor.authorZebger, Ingo
dc.contributor.authorHildebrandt, Peter
dc.contributor.authorTodorovic, Smilja
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblMDPI - Multidisciplinary Digital Publishing Institute
dc.date.accessioned2022-07-20T22:30:11Z
dc.date.available2022-07-20T22:30:11Z
dc.date.issued2021-08-02
dc.descriptionFunding Information: Funding: This research was funded by FEDER funds through COMPETE2020—Programa Opera-cional Competitividade e Internacionalização (POCI) and by national funds through FCT—Fundacão para a Ciência e a Tecnologia, grant Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular). S.T. acknowledges grant PTDC/BTM-SAL/29507/2017, C.M.S. acknowledges grant PTDC/BIA-BFS/31026/2017 project, and C.B. acknowledges fellowship 2020.05017.BD all funded by FCT. G.C., I.Z., and P.H. are grateful for funding from the Einstein Foundation Berlin (grant number EVF-2016-277). This work was also supported through the cluster of excellence “UniSysCat“ funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy-EXC2008/1-390540038 and the SPP 1927 ”Iron Sulfur for Life”—ZE 510/2-2 (IZ). The APC was funded by the TIMB3 project, European Union’s Horizon 2020 research and innovation program, under grant agreement No 810856. Funding Information: This research was funded by FEDER funds through COMPETE2020?Programa Opera-cional Competitividade e Internacionaliza??o (POCI) and by national funds through FCT?Fundac?o para a Ci?ncia e a Tecnologia, grant Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular). S.T. acknowledges grant PTDC/BTM-SAL/29507/2017, C.M.S. acknowledges grant PTDC/BIA-BFS/31026/2017 project, and C.B. acknowledges fellowship 2020.05017.BD all funded by FCT. G.C., I.Z., and P.H. are grateful for funding from the Einstein Foundation Berlin (grant number EVF-2016-277). This work was also supported through the cluster of excellence ?UniSysCat? funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Founda-tion) under Germany?s Excellence Strategy-EXC2008/1-390540038 and the SPP 1927 ?Iron Sulfur for Life??ZE 510/2-2 (IZ). The APC was funded by the TIMB3 project, European Union?s Horizon 2020 research and innovation program, under grant agreement No 810856. Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
dc.description.abstractVibrational spectroscopy and in particular, resonance Raman (RR) spectroscopy, can provide molecular details on metalloproteins containing multiple cofactors, which are often challenging for other spectroscopies. Due to distinct spectroscopic fingerprints, RR spectroscopy has a unique capacity to monitor simultaneously and independently different metal cofactors that can have particular roles in metalloproteins. These include e.g., (i) different types of hemes, for instance hemes c, a and a3 in caa3-type oxygen reductases, (ii) distinct spin populations, such as electron transfer (ET) low-spin (LS) and catalytic high-spin (HS) hemes in nitrite reductases, (iii) different types of Fe-S clusters, such as 3Fe-4S and 4Fe-4S centers in di-cluster ferredoxins, and (iv) bi-metallic center and ET Fe-S clusters in hydrogenases. IR spectroscopy can provide unmatched molecular details on specific enzymes like hydrogenases that possess catalytic centers coordinated by CO and CN− ligands, which exhibit spectrally well separated IR bands. This article reviews the work on metalloproteins for which vibrational spectroscopy has ensured advances in understanding structural and mechanistic properties, including multiple heme-containing proteins, such as nitrite reductases that house a notable total of 28 hemes in a functional unit, respiratory chain complexes, and hydrogenases that carry out the most fundamental functions in cells.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent2723467
dc.identifier.doi10.3390/molecules26164852
dc.identifier.issn1420-3049
dc.identifier.otherPURE: 42191757
dc.identifier.otherPURE UUID: 583a0973-630f-4e34-9c02-4bc0aef228bc
dc.identifier.otherScopus: 85112698979
dc.identifier.otherPubMed: 34443440
dc.identifier.urihttp://hdl.handle.net/10362/142215
dc.identifier.urlhttps://www.scopus.com/pages/publications/85112698979
dc.language.isoeng
dc.peerreviewedyes
dc.subjectFe-S clusters
dc.subjectHeme proteins
dc.subjectHydrogenases
dc.subjectIR
dc.subjectMetalloproteins
dc.subjectResonance Raman spectroscopy
dc.subjectVibrational spectroscopy
dc.subjectAnalytical Chemistry
dc.subjectChemistry (miscellaneous)
dc.subjectMolecular Medicine
dc.subjectPharmaceutical Science
dc.subjectDrug Discovery
dc.subjectPhysical and Theoretical Chemistry
dc.subjectOrganic Chemistry
dc.titleMolecular details on multiple cofactor containing redox metalloproteins revealed by infrared and resonance raman spectroscopiesen
dc.typejournal article
degois.publication.issue16
degois.publication.titleMolecules
degois.publication.volume26
dspace.entity.typePublication
rcaap.rightsopenAccess

Ficheiros

Principais
A mostrar 1 - 1 de 1
Miniatura
Nome:
artigo1.pdf
Tamanho:
2.6 MB
Formato:
Adobe Portable Document Format
Ver/Abrir

Coleções

Home collection (ITQB)