The Solution Structure of a Tetraheme Cytochrome from Shewanella frigidimarina Reveals a Novel Family Structural Motif

Vitor Paixão, Carlos Alberto Gomes Salgueiro, Lorraine Brennan, Graeme A. Reid, Stephen K. Chapman, D.L. Turner

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The bacteria belonging to the genus Shewanella are facultative anaerobes that utilize a variety of terminal electron acceptors which includes soluble and insoluble metal oxides. The tetraheme c-type cytochrome isolated during anaerobic growth of Shewanella frigidimarina NCIMB400 (Sfc) contains 86 residues and is involved in the Fe(III) reduction pathways. Although the functional properties of Sfc redox centers are quite well described, no structures are available for this protein. In this work, we report the solution structure of the reduced form of Sfc. The overall fold is completely different from those of the tetraheme cytochromes c(3) and instead has similarities with the tetraheme cytochrome recently isolated from Shewanella oneidensis (Soc). Comparison of the tetraheme cytochromes from Shewanella shows a considerable diversity in their primary structure and heme reduction potentials, yet they have highly conserved heme geometry, as is the case for the family of tetraheme cytochromes isolated from Desulfovibrio spp.
Original languageEnglish
Pages (from-to)11973-11980
Number of pages8
JournalBiochemistry
Volume47
Issue number46
DOIs
Publication statusPublished - 18 Nov 2008

Keywords

  • Hemoglobin
  • Iron compounds

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