The annotation of more than 200 genes involved in catabolism and

The annotation of more than 200 genes involved in catabolism and respiration in the genome of the anammox bacterium Kuenenia stuttgartiensis, together with the abundance of 61 genes encoding c-type cytochrome proteins, reflects the complexity of the anammox metabolism and implies the presence of a branched and versatile respiratory chain [5]. This complexity is further confirmed by the genome assemblies

of two more anammox species that were recently reported (Scalindua profunda[6]; strain KSU-1 [7]). Although c-type cytochrome proteins seem to play a key role in the unique anammox metabolism, the maturation pathway of functional c-type cytochrome holoforms has not been explored. Cytochrome c maturation describes the post-translational process by which b-type Selleck Captisol hemes (Fe-protoporphyrin IX) are covalently attached to the apoproteins resulting in functional c-type cytochromes. After synthesis, apocytochrome c and heme molecules are independently translocated

across the energy-transducing membrane into the bacterial periplasm, the mitochondrial intermembrane space or the thylakoid lumen. Ferric iron of heme(s) and cysteine https://www.selleckchem.com/products/H-89-dihydrochloride.html residues of apocytochrome c are reduced and subsequent thioether linkage formation occurs Doramapimod clinical trial between the heme vinyl groups and the CX2-4CH sulfhydryls of apocytochrome c, leading to the functional holoform [8]. Three distinct cytochrome c maturation pathways (Systems I, II and III) have been described, each comprising system-specific assembly protein complexes; these biogenesis systems occur in a wide variety of organisms with a complex and unpredictable phylogenetic distribution [9]. Figure 1 Maturation System II of c -type cytochrome proteins in anammox bacteria. A: Schematic drawing of the anammox cell and the maturation system machinery depicted on it. The dotted trapezoid is zoomed-in in FigureĀ  2B. 1: cell wall; 2: cytoplasmic membrane; 3: intracytoplasmic membrane; 4: anammoxosome membrane; i: paryphoplasm; ii: riboplasm; iii: anammoxosome;

iv: nucleoid; v: ribosome. B: 3D illustration of cytochrome c maturation System II localized within the anammoxosome membrane. Apocytochrome c is translocated to the p-side of the membrane via the Sec pathway. CcsA-CcsB complex, forming the heme channel however entry, is tethered within the anammoxosome membrane. Heme is, thus, translocated within the anammoxosome. Concurrently, reducing equivalents from the n-side of the cell are fed to a disulfide bond cascade that proceeds from DsbD to CcsX. The latter, being a dedicated thiol-disulfide oxidoreductase, reduces the cysteine residues of apocytochrome c, and eventually spontaneous ligation for the thioether linkages formation between the apoprotein and its cofactor takes place. Green pie depicts apocytochrome c; red triangle depicts heme molecule.

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