NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation

M Pessanha, L Brennan, AV Xavier, PM Cuthbertson, Graeme A Reid, Stephen Chapman, DL Turner, CA Salgueiro

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    Abstract

    The tetrahaem cytochrome isolated during anaerobic growth of Shewanella frigidimarina NCIMB400 is a small protein (86 residues) involved in electron transfer to Fe(III), which can be used as a terminal respiratory oxidant by this bacterium. A 3D solution structure model of the reduced form of the cytochrome has been determined using NMR data in order to determine the relative orientation of the haems. The haem core architecture of S. frigidimarina tetrahaem cytochrome differs from that found in all small tetrahaem cytochromes c(3) so far isolated from strict anaerobes, but has some similarity to the N-terminal cytochrome domain of flavocytochrome c(3) isolated from the same bacterium. NMR signals obtained for the four haems of S. frigidimarina tetrahaem cytochrome at all stages of oxidation were cross-assigned to the solution structure using the complete network of chemical exchange connectivities. Thus, the order in which each haem in the structure becomes oxidised was determined. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)8-13
    Number of pages6
    JournalFEBS Letters
    Volume489
    Issue number1
    DOIs
    Publication statusPublished - 26 Jan 2001

    Keywords

    • C(3)
    • REDOX
    • DESULFURICANS ATCC-27774
    • multihaem cytochrome
    • FLAVOCYTOCHROME
    • CRYSTAL-STRUCTURE
    • Shewanella
    • GIGAS
    • PUTREFACIENS MR-1
    • DESULFOVIBRIO-VULGARIS HILDENBOROUGH
    • PROTON THRUSTER
    • ring current
    • iron-respiration
    • nuclear magnetic resonance
    • FUMARATE REDUCTASE

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