Overexpression of multi-heme C-type cytochromes
نویسندگان
چکیده
منابع مشابه
High-molecular-mass multi-c-heme cytochromes from Methylococcus capsulatus bath.
The polypeptide and structural gene for a high-molecular-mass c-type cytochrome, cytochrome c553O, was isolated from the methanotroph Methylococcus capsulatus Bath. Cytochrome c553O is a homodimer with a subunit molecular mass of 124,350 Da and an isoelectric point of 6. 0. The heme c concentration was estimated to be 8.2 +/- 0.4 mol of heme c per subunit. The electron paramagnetic resonance sp...
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Cytochromes c are hemoproteins, with the prosthetic group covalently linked to the apoprotein, which function as electron carriers. A class of cytochromes c is defined by a CXXCH heme-binding motif where the cysteines form thioether bonds with the vinyl groups of heme. Plastids are known to contain up to three cytochromes c. The membrane-bound cytochrome f and soluble cytochrome c6 operate in p...
متن کاملBiogenesis of mitochondrial c-type cytochromes.
Cytochromes c and c1 are essential components of the mitochondrial respiratory chain. In both cytochromes the heme group is covalently linked to the polypeptide chain via thioether bridges. The location of the two cytochromes is in the intermembrane space; cytochrome c is loosely attached to the surface of the inner mitochondrial membrane, whereas cytochrome c1 is firmly anchored to the inner m...
متن کاملControl of DegP-dependent degradation of c-type cytochromes by heme and the cytochrome c maturation system in Escherichia coli.
c-Type cytochromes are located partially or completely in the periplasm of gram-negative bacteria, and the heme prosthetic group is covalently bound to the protein. The cytochrome c maturation (Ccm) multiprotein system is required for transport of heme to the periplasm and its covalent linkage to the peptide. Other cytochromes and hemoglobins contain a noncovalently bound heme and do not requir...
متن کاملElectrophoretic behavior of mammalian-type cytochromes c.
Anomalous boundaries resulting from the binding of a buffer constituent give the appearance of electrophoretic inhomogeneity to pure crystalline native monomeric cytochromes c from 10 species (man, horse, hog, guanaco, Pekin duck, pigeon, turkey, tuna, a moth (Samia cynfhia), and the screw worm fly). The electrophoretic patterns depend on the particular cytochrome c used and its concentration, ...
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ژورنال
عنوان ژورنال: BioTechniques
سال: 2005
ISSN: 0736-6205,1940-9818
DOI: 10.2144/05382pt01