The process of maturation of multiheme proteins is not yet well known, while that of
monoheme ones has been relatively well investigated. Two kinds of partly unfolded …

Shewanella are renowned for their ability to respire on a wide range of electron acceptors,
which has been partially accredited to the presence of a large number of the c-type …

Integrated studies that address proteins structure and function in the new era of systems
biology and genomics often require the application of high-throughput approaches for …

Homologous cytochromes c 5 from a mesophile, Shewanella amazonensis (SA cyt c 5), and
a psychrophile, Shewanella violacea (SV cyt c 5), were compared to elucidate the molecular …

The genes of tetraheme cytochrome c3 and hexadecaheme high-molecular-weight
cytochrome c from Desulfovibrio vulgaris could be overexpressed as holoproteins in …

The structure of a novel c7‐type cytochrome domain that has two bishistidine coordinated
hemes and one heme with histidine, methionine coordination (where the sixth ligand is a …

Crystals of the tetraheme cytochrome c3 from sulfate‐reducing bacteria Desulfovibrio gigas
(Dg)(MW 13 kDa, 111 residues, four heme groups) were obtained and X‐ray diffraction data …

Multiheme cytochromes c are important in electron transfer pathways in reduction of both
soluble and insoluble Fe (III) by Geobacter sulfurreducens. We determined the crystal …

Cytochromes-c are ubiquitous heme proteins with enormous impact at the cellular level,
being key players in metabolic processes such as electron transfer chains and apoptosis …

Tetraheme cytochrome c 3 (cyt c 3) exhibits extremely low reduction potentials and unique
properties. Since axial ligands should be the most important factors for this protein, every …