Cloning and sequence analysis of the gene encoding Methylophilus methylotrophus cytochrome c'', a unique protein with a perpendicular orientation of the histidinyl ligands

Nicholas J. Price, Erik Vijgenboom, Graça Ribeiro, João V. Costa, Gerard W. Canters, Helena Santos

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Cytochrome c'' from Methylophilus methylotrophus is an unusual monohaem protein that undergoes a major redox-linked spin-state transition: one of the two axial histidines bound to the iron in the oxidised form is detached upon reduction and a proton is taken up. A 3.5-kb DNA fragment, containing the gene encoding cytochrome c'' (cycA), has been cloned and sequenced. The cytochrome c'' gene codes for a pre-protein with a typical prokaryotic 20-residue signal sequence, suggesting that the protein is synthesised as a precursor which is processed during its secretion into the periplasm. The C-terminus of cytochrome c'' has homology with the corresponding region of an oxygen-binding haem protein (SHP) from phototrophically grown Rhodobacter sphaeroides. SHP is similar in size and in the location of its haem-binding site. Immediately downstream from cytochrome c'' a second open reading frame (ORF) codes for a 23-kDa protein with similarity to the cytochrome b-type subunit of Ni-Fe hydrogenase. The possibility of coordinated expression of cycA and this ORF is discussed. Copyright (C) 1999 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)55-61
Number of pages7
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1413
Issue number1
DOIs
Publication statusPublished - 1 Sep 1999

Keywords

  • Cytochrome c''
  • Methylophilus methylotrophus
  • Nucleotide sequencing
  • Redox protein

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