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Resonance assignments of cytochrome MtoD from the extracellular electron uptake pathway of sideroxydans lithotrophicus ES-1

dc.contributor.authorCoelho, Anaísa
dc.contributor.authorSilva, José M.
dc.contributor.authorCantini, Francesca
dc.contributor.authorPiccioli, Mario
dc.contributor.authorLouro, Ricardo O.
dc.contributor.authorPaquete, Catarina M.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblSpringer
dc.date.accessioned2025-05-07T21:19:24Z
dc.date.available2025-05-07T21:19:24Z
dc.date.issued2024
dc.descriptionFunding Information: This work benefited from access to CERM/CIRMMP, the Instruct-ERIC Italy center, and CERMAX, ITQB-NOVA, Oeiras, Portugal with equipment funded by FCT - Funda\u00E7\u00E3o para a Ci\u00EAncia e a Tecnologia, I.P. (FCT), project AAC 01/SAICT/2016. Financial support was provided by European EC Horizon2020 TIMB3 (Project 810856) Instruct-ERIC (PID22135). Financial support was also provided by Project MOSTMICRO-ITQB with refs UIDB/04612/2020 and UIDP/04612/2020, and projects PTDC/BIA-BQM/4143/2021 and PD/BD/135153/2017 integrated in the PhD Programme in NMR applied to chemistry, materials and biosciences (PD/00065/2013). Funding Information: Open access funding provided by Universit\u00E0 degli Studi di Firenze within the CRUI-CARE Agreement. Publisher Copyright: © The Author(s) 2024.
dc.description.abstractThe contribution of Fe(II)-oxidizing bacteria to iron cycling in freshwater, groundwater, and marine environments has been widely recognized in recent years. These organisms perform extracellular electron transfer (EET), which constitutes the foundations of bioelectrochemical systems for the production of biofuels and bioenergy. It was proposed that the Gram-negative bacterium Sideroxydans lithotrophicus ES-1 oxidizes soluble ferrous Fe(II) at the surface of the cell and performs EET through the Mto redox pathway. This pathway is composed by the periplasmic monoheme cytochrome MtoD that is proposed to bridge electron transfer between the cell exterior and the cytoplasm. This makes its functional and structural characterization, as well as evaluating the interaction process with its physiological partners, essential for understanding the mechanisms underlying EET. Here, we report the complete assignment of the heme proton and carbon signals together with a near-complete assignment of 1H, 13C and 15N backbone and side chain resonances for the reduced, diamagnetic form of the protein. These data pave the way to identify and structurally map the molecular interaction regions between the cytochrome MtoD and its physiological redox partners, to explore the EET processes of S. lithotrophicus ES-1.en
dc.description.versionpublishersversion
dc.description.versioninpress
dc.format.extent1468792
dc.identifier.doi10.1007/s12104-024-10180-8
dc.identifier.issn1874-2718
dc.identifier.otherPURE: 99908831
dc.identifier.otherPURE UUID: 3908f254-7bb1-4e4a-963a-edd52c59a601
dc.identifier.otherScopus: 85195255574
dc.identifier.urihttp://hdl.handle.net/10362/182746
dc.identifier.urlhttps://www.scopus.com/pages/publications/85195255574
dc.language.isoeng
dc.peerreviewedyes
dc.subjectCytochromes
dc.subjectExtracellular electron transfer
dc.subjectMtoD
dc.subjectNMR resonance assignment
dc.subjectRing current shifts
dc.subjectStructural Biology
dc.subjectBiochemistry
dc.subjectSDG 6 - Clean Water and Sanitation
dc.subjectSDG 14 - Life Below Water
dc.titleResonance assignments of cytochrome MtoD from the extracellular electron uptake pathway of sideroxydans lithotrophicus ES-1en
dc.typejournal article
degois.publication.titleBiomolecular Nmr Assignments
dspace.entity.typePublication
rcaap.rightsopenAccess

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