NMR redox studies of flavocytochrome c3 from Shewanella frigidimarina

Miguel Pessanha, David L Turner, Emma L Rothery, Katherine L Pankhurst, Graeme A Reid, Stephen K Chapman, Antonio V Xavier, Carlos A Salgueiro

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    Abstract

    Flavocytochrome c(3) is a periplasmic fumarate reductase with M-r 63.8 kDa, isolated from Shewanella frigidimarina NCIMB400. NMR spectroscopy was tested for its potential to elucidate the oxidation profile of each of the four haem groups in the enzyme, using the strategy developed previously to perform the thermodynamic characterization of small tetrahaem cytochromes (FEBS Lett. 314 (1992) 155). This work shows that, despite the large size of the protein, 2D-NMR NOESY experiments can be used to obtain the network of chemical exchange connectivities, between the signals of specific haem groups in sequential oxidation stages. (C) 2003 Elsevier Science B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)379-381
    Number of pages3
    JournalInorganica Chimica Acta
    Volume356
    DOIs
    Publication statusPublished - 3 Dec 2003

    Keywords

    • ENERGY TRANSDUCTION
    • paramagnetic shifts
    • DESULFOVIBRIO-VULGARIS
    • multihaem
    • RESPIRATION
    • Shewanella
    • electron tranfer protein
    • PUTREFACIENS MR-1
    • ELECTRON-TRANSFER
    • COOPERATIVITY
    • flavocytochrome
    • NCIMB400
    • NMR
    • FUMARATE REDUCTASE
    • CYTOCHROME C(3)
    • HEME CORE

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