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• W1974440975 abstract "Pyruvate ferredoxin oxidoreductase (POR) from the hyperthermophilic archaeon Pyrococcus furiosus (Pf) catalyzes the final oxidative step in carbohydrate fermentation in which pyruvate is oxidized to acetyl-CoA and CO2, coupled to the reduction of ferredoxin (Fd). POR is composed of two ‘catalytic units' of molecular mass ∼120 kDa. Each unit consists of four subunits, αβγδ, with masses of approximately 44, 36, 20, and 12 kDa, respectively, and contains at least two [4Fe-4S] clusters. The precise mechanism of catalysis and the role of the individual subunits are not known. The gene encoding the δ-subunit of Pf POR has been expressed in E. coli, and the protein was purified after reconstitution with iron and sulfide. The reconstituted δ-subunit (recPOR-δ) is monomeric with a mass of 11 879 ± 1.2 Da as determined by mass spectrometry, in agreement with that predicted from the gene sequence. Purified recPOR-δ contains 8 Fe mol/mol and remained intact when incubated at 85 °C for 2 h, as judged by its visible absorption properties. The reduced form of the protein exhibited an EPR spectrum characteristic of two, spin−spin interacting [4Fe-4S]1+ clusters. When compared with the EPR properties of the reduced holoenzyme, the latter was shown to contain a third [4Fe-4S]1+ cluster in addition to the two within the δ-subunit. The reduction potential of the two 4Fe clusters in isolated recPOR-δ (−403 ± 8 mV at pH 8.0 and 24 °C) decreased linearly with temperature (−1.55 mV/°C) up to 82 °C. RecPOR-δ replaced Pf Fd as an in vitro electron carrier for two oxidoreductases from Pf, POR and Fd:NADP oxidoreductase, and the POR holoenzyme displayed a higher apparent affinity for its own subunit (apparent Km = 1.0 μM at 80 °C) than for Fd (apparent Km = 4.4 μM). The molecular and spectroscopic properties and amino acid sequence of the isolated δ-subunit suggest that it evolved from an 8Fe-type Fd by the addition of ∼40 residues at the N-terminus, and that this extension enabled it to interact with additional subunits within POR." @default.
• W1974440975 created "2016-06-24" @default.
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• W1974440975 date "1998-08-28" @default.
• W1974440975 modified "2023-10-03" @default.
• W1974440975 title "The δ-Subunit of Pyruvate Ferredoxin Oxidoreductase from <i>Pyrococcus</i> <i>furiosus</i> Is a Redox-Active, Iron−Sulfur Protein: Evidence for an Ancestral Relationship with 8Fe-Type Ferredoxins" @default.
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• W1974440975 doi "https://doi.org/10.1021/bi980979p" @default.
• W1974440975 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9737861" @default.
• W1974440975 hasPublicationYear "1998" @default.
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