1H21

A novel iron centre in the split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774

Replaces:  1DDC

Summary for 1H21

• Entry DOI: 10.2210/pdb1h21/pdb
• Related: 1DDC
• Descriptor: SPLIT-SORET CYTOCHROME C, HEME C (3 entities in total)
• Functional Keywords: cytochrome, dimeric di-heme cytochrome, stacked heme arrangement, novel fold, novel iron-sulfur centre, electron transport, sulfate respiration
• Biological source: DESULFOVIBRIO DESULFURICANS
• Total number of polymer chains: 4
• Total formula weight: 112705.90

Authors

Abreu, I.A.,Lourenco, A.I.,Xavier, A.V.,Legall, J.,Coelho, A.V.,Matias, P.M.,Pinto, D.M.,Carrondo, M.A.,Teixeira, M.,Saraiva, L.M. (deposition date: 2002-07-30, release date: 2003-02-20, Last modification date: 2011-07-13)

Primary citation

Abreu, I.A.,Lourenco, A.I.,Xavier, A.V.,Legall, J.,Coelho, A.V.,Matias, P.M.,Pinto, D.M.,Armenia Carrondo, M.,Teixeira, M.,Saraiva, L.M.
A Novel Iron Centre in the Split-Soret Cytochrome C from Desulfovibrio Desulfuricans Atcc 27774
J.Biol.Inorg.Chem., 8:360-, 2003

PubMed Abstract: The facultative sulfate/nitrate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 harbours a split-Soret cytochrome c. This cytochrome is a homodimeric protein, having two bis-histidinyl c-type haems per monomer. It has an unique architecture at the haem domain: each haem has one of the coordinating histidines provided by the other monomer, and in each monomer the haems are parallel to each other, almost in van der Waals contact. This work reports the cloning and sequencing of the gene encoding for this cytochrome and shows, by transcriptional analysis, that it is more expressed in nitrate-grown cells than in sulfate-grown ones. In addition, the gene-deduced amino acid sequence revealed two new cysteine residues that could be involved in the binding of a non-haem iron centre. Indeed, the presence of a novel type of an iron-sulfur centre (possibly of the [2Fe-2S] type) was demonstrated by EPR spectroscopy, and putative models for its localization and structure in the cytochrome molecule are proposed on the basis of the so-far-known 3D crystallographic structure of the aerobically purified split-Soret cytochrome, which lacks this centre.

PubMed: 12589573
DOI: 10.1007/S00775-002-0426-3

Experimental method

X-RAY DIFFRACTION (2.5 Å)