
The High-Molecular-Weight Cytochrome c Cyc2 of Acidithiobacillus ferrooxidans Is an Outer Membrane Protein
Author(s) -
Andrés Yarzábal,
Gaël Brasseur,
Jeanine Ratouchniak,
Karen Lund,
Danielle Lemesle-Meunier,
John A. DeMoss,
Violaine Bonnefoy
Publication year - 2002
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.184.1.313-317.2002
Subject(s) - spheroplast , bacterial outer membrane , biology , cytochrome , membrane , ferrous , biochemistry , cytochrome c , cytochrome b , cytoplasm , electron acceptor , membrane protein , acidithiobacillus , acidithiobacillus ferrooxidans , mitochondrion , enzyme , chemistry , gene , bioleaching , mitochondrial dna , organic chemistry , escherichia coli , copper
A high-molecular-weight c-type cytochrome, Cyc2, and a putative 22-kDa c-type cytochrome were detected in the membrane fraction released during spheroplast formation from Acidithiobacillus ferrooxidans. This fraction was enriched in outer membrane components and devoid of cytoplasmic membrane markers. The genetics, as well as the subcellular localization of Cyc2 at the outer membrane level, therefore make it a prime candidate for the initial electron acceptor in the respiratory pathway between ferrous iron and oxygen.