Characterisation of pdus, the pdu metabolosome corrin reductase, and evidence of substructural organisation within the bacterial microcompartment

Parsons, Joshua B., Lawrence, Andrew D., Mclean, Kirsty J., Munro, Andrew W., Rigby, Stephen E.J. and Warren, Martin J. ORCID: https://orcid.org/0000-0002-6028-6456 (2010) Characterisation of pdus, the pdu metabolosome corrin reductase, and evidence of substructural organisation within the bacterial microcompartment. PLoS One, 5 (11). ISSN 1932-6203

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Abstract

PduS is a corrin reductase and is required for the reactivation of the cobalamin-dependent diol dehydratase. It is one component encoded within the large propanediol utilisation (pdu) operon, which is responsible for the catabolism of 1,2-propanediol within a self-assembled proteinaceous bacterial microcompartment. The enzyme is responsible for the reactivation of the cobalamin coenzyme required by the diol dehydratase. The gene for the cobalamin reductase from Citrobacter freundii (pduS) has been cloned to allow the protein to be overproduced recombinantly in E. coli with an Nterminal His-tag. Purified recombinant PduS is shown to be a flavoprotein with a non-covalently bound FMN that also contains two coupled [4Fe-4S] centres. It is an NADH-dependent flavin reductase that is able to mediate the one-electron reductions of cob(III)alamin to cob(II)alamin and cob(II)alamin to cob(I)alamin. The [4Fe-4S] centres are labile to oxygen and their presence affects the midpoint redox potential of flavin. Evidence is presented that PduS is able to bind cobalamin, which is inconsistent with the view that PduS is merely a flavin reductase. PduS is also shown to interact with one of the shell proteins of the metabolosome, PduT, which is also thought to contain an [Fe-S] cluster. PduS is shown to act as a corrin reductase and its interaction with a shell protein could allow for electron passage out of the bacterial microcompartment.

Item Type: Article
Uncontrolled Keywords: biochemistry, genetics and molecular biology(all),agricultural and biological sciences(all),general ,/dk/atira/pure/subjectarea/asjc/1300
Faculty \ School: Faculty of Science
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Depositing User: LivePure Connector
Date Deposited: 20 Sep 2022 15:30
Last Modified: 25 Oct 2022 00:14
URI: https://ueaeprints.uea.ac.uk/id/eprint/88520
DOI: 10.1371/journal.pone.0014009

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