Logo do repositório
 
Publicação

Magnetic interactions between metal sites in complex enzymes

2025-08Recensão Acesso aberto
Ver registo simples
dc.contributor.authorMaiti, Biplab K.
dc.contributor.authorMoura, Isabel
dc.contributor.authorMoura, José J.G.
dc.contributor.institutionLAQV@REQUIMTE
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.pblSpringer
dc.date.accessioned2025-09-03T21:53:52Z
dc.date.available2025-09-03T21:53:52Z
dc.date.issued2025-08
dc.descriptionOpen access funding provided by FCT|FCCN (b-on). Funding from DST\u2012SERB, India for the CRG grant (CRG/2022/005673). Publisher Copyright: © The Author(s) 2025.
dc.description.abstractMagnetic interactions between iron–sulfur (Fe/S) clusters and transition metal centers such as nickel, molybdenum, and copper play a central role in the function of key metalloenzymes. These interactions, which arise from electronic coupling, spin exchange, and spatial arrangement, directly influence redox behavior and catalytic efficiency. This review highlights three distinct complex enzymes—[NiFe] hydrogenases, mononuclear molybdenum-containing xanthine oxidase (XO) family, and [NiFe] and [MoCu] carbon monoxide dehydrogenases (CODHs)—as paradigms for understanding (Fe/S)-metal center interactions. In [NiFe] hydrogenases, (Fe/S) clusters serve as electron relays that magnetically interact with the catalytic [NiFe] active site. In XO-type enzymes, a mononuclear Mo center is functionally and magnetically coupled to nearby Fe/S clusters, modulating substrate reduction and electron transfer. Similarly, in CODHs, both [NiFe]—and [MoCu]-dependent variants exhibit strong magnetic communication between metal active sites and surrounding Fe/S clusters, crucial for CO2/CO interconversion. Advanced spectroscopic approaches, particularly electron paramagnetic resonance (EPR) and related techniques, combined with theoretical modelling, have provided deep insights into the electronic structures and dynamic interactions within these metalloenzymes. Understanding these magnetic interactions not only sheds light on fundamental electron-transfer and enzymatic mechanisms but also guides the design of bioinspired catalysts and energy-conversion technologies.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent16
dc.format.extent2058163
dc.identifier.doi10.1007/s00775-025-02120-1
dc.identifier.issn0949-8257
dc.identifier.otherPURE: 128620870
dc.identifier.otherPURE UUID: b17822f7-32b7-4cd3-aed8-d295089625d3
dc.identifier.otherScopus: 105011393757
dc.identifier.otherPubMed: 40705057
dc.identifier.urihttp://hdl.handle.net/10362/187506
dc.identifier.urlhttps://www.scopus.com/pages/publications/105011393757
dc.language.isoeng
dc.peerreviewedyes
dc.relationFunding Information: info:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBTA-BTA%2F0935%2F2020/PT
dc.relationinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50006%2F2020/PT
dc.relationAssociated Laboratory for Green Chemistry - Clean Technologies and Processes
dc.relationAssociated Laboratory for Green Chemistry - Clean Technologies and Processes
dc.subjectAldehyde oxidoreductase
dc.subjectCO dehydrogenase
dc.subjectElectron transfer
dc.subjectIron–sulfur centers
dc.subjectMagnetic interactions
dc.subject[NiFe] Hydrogenase
dc.subjectBiochemistry
dc.subjectInorganic Chemistry
dc.titleMagnetic interactions between metal sites in complex enzymesen
dc.typereview
degois.publication.firstPage329
degois.publication.issue4-5
degois.publication.lastPage344
degois.publication.titleJournal of Biological Inorganic Chemistry
degois.publication.volume30
dspace.entity.typePublication
oaire.awardNumberUIDB/50006/2020
oaire.awardNumberUIDP/50006/2020
oaire.awardTitleAssociated Laboratory for Green Chemistry - Clean Technologies and Processes
oaire.awardTitleAssociated Laboratory for Green Chemistry - Clean Technologies and Processes
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50006%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F50006%2F2020/PT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
relation.isProjectOfPublicationadc84c24-ba1d-4bcd-b753-2128ce9a5faa
relation.isProjectOfPublication4d9a4d40-4803-4f3a-976b-d6eaaef42510
relation.isProjectOfPublication.latestForDiscovery4d9a4d40-4803-4f3a-976b-d6eaaef42510

Ficheiros

Principais
A mostrar 1 - 1 de 1
Miniatura
Nome:
s00775-025-02120-1.pdf
Tamanho:
1.96 MB
Formato:
Adobe Portable Document Format
Ver/Abrir

Coleções

Home collection (FCT)