Logo do repositório
 
Publicação

Structure and redox properties of the diheme electron carrier cytochrome c4 from Pseudomonas aeruginosa

2020-02-01Artigo científico Acesso aberto
Ver registo simples
dc.contributor.authorCarpenter, Jessica M.
dc.contributor.authorZhong, Fangfang
dc.contributor.authorRagusa, Michael J.
dc.contributor.authorLouro, Ricardo O.
dc.contributor.authorHogan, Deborah A.
dc.contributor.authorPletneva, Ekaterina V.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.pblElsevier
dc.date.accessioned2020-01-22T23:39:38Z
dc.date.available2020-01-22T23:39:38Z
dc.date.issued2020-02-01
dc.description.abstractAt low oxygen concentrations, respiration of Pseudomonas aeruginosa (Pa) and other bacteria relies on activity of cytochrome cbb3 oxidases. A diheme cytochrome c4 (cyt c4) donates electrons to Pa cbb3 oxidases to enable oxygen reduction and proton pumping by these enzymes. Given the importance of this redox pathway for bacterial pathogenesis, both cyt c4 and cbb3 oxidase are potential targets for new antibacterial strategies. The structural information about these two proteins, however, is scarce, and functional insights for Pa and other bacteria have been primarily drawn from analyses of the analogous system from Pseudomonas stutzeri (Ps). Herein, we describe characterization of structural and redox properties of cyt c4 from Pa. The crystal structure of Pa cyt c4 has revealed that this protein is organized in two monoheme domains. The interdomain interface is more hydrophobic in Pa cyt c4, and the protein surface does not show the dipolar distribution of charges found in Ps cyt c4. The reduction potentials of the two hemes are similar in Pa cyt c4 but differ by about 100 mV in Ps cyt c4. Analyses of structural models of these and other cyt c4 proteins suggest that multiple factors contribute to the potential difference of the two hemes in these proteins, including solvent accessibility of the heme group, the distribution of surface charges, and the nature of the interdomain interface. The distinct properties of cyt c4 proteins from closely-related Pa and Ps bacteria emphasize the importance of examining the cbb3/cyt c4 redox pathway in multiple species.en
dc.description.versionpreprint
dc.description.versionpublished
dc.format.extent1779110
dc.identifier.doi10.1016/j.jinorgbio.2019.110889
dc.identifier.issn0162-0134
dc.identifier.otherPURE: 16465636
dc.identifier.otherPURE UUID: 85b2419a-22c8-4d5e-b2de-b248fc42f0d3
dc.identifier.otherScopus: 85074564188
dc.identifier.otherPubMed: 31707335
dc.identifier.urihttp://hdl.handle.net/10362/91642
dc.identifier.urlhttps://www.scopus.com/pages/publications/85074564188
dc.language.isoeng
dc.peerreviewedyes
dc.subjectcbb oxidase
dc.subjectElectron transfer
dc.subjectMultiheme proteins
dc.subjectRedox partners
dc.subjectReduction potentials
dc.subjectBiochemistry
dc.subjectInorganic Chemistry
dc.titleStructure and redox properties of the diheme electron carrier cytochrome c4 from Pseudomonas aeruginosaen
dc.typejournal article
degois.publication.titleJournal of Inorganic Biochemistry
degois.publication.volume203
dspace.entity.typePublication
rcaap.rightsrestrictedAccess

Ficheiros

Principais
A mostrar 1 - 1 de 1
Miniatura
Nome:
structure_c4_JIB_revision_si_evp_092519.pdf
Tamanho:
1.7 MB
Formato:
Adobe Portable Document Format
Ver/Abrir

Coleções

Home collection (ITQB)