Cytochrome c 7

Cytocrhome c 7 (Cc7) is a three heme-containing protein derived from the sulfur-reducing bacterium Desulfuromonas acetoxidans. Cc7 is located in the mitochondrial intermembrane space of the bacteria where it plays a role in the electron-transfer mechanism ^[1]. Desulfuromonas acetoxidans bacteria have evolved to obtain their energy from anaerobic sulfure respiration, thus requiring organic disulfide compounds, such as thiosulfate, sulfur, sulfite, or sulfate, as their electron acceptors^[2]. This gives Cc7 a very unique ability that interests a lot of researchers as of late: the fact that this protein is able to reduce disulfide compounds down to hydrogen sulfide, which in turn reacts with heavy metal ions to form low-toxicity metal sulfides^[3]. To apply this characteristic, researchers hope to create possible applications to use these bacteria in decontamination of environments that are polluted with toxic heavy metals. Because of the insolubility of the metal sulfides, removing them from the environment will be simpler and cheaper than current heavy metal toxic waste filtration operations^[4].

Structural Components

Cc7 is a single polypeptide chain 68 residues total containing three heme groups. The polypeptide strand has one alpha helix 4 residues in length and two beta strands 2 residues in length. The heme groups are labelled as I, III, and IV,

Function

Cc7 is a sulfur terminal reductase, that is, it reduces a sulfur-containing compound into a sulfide to generate electrons to be used in electron transport chain.

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.