Electrophoretic Behavior of Mammalian-type Cytochromes c
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چکیده
منابع مشابه
Electrophoretic 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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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...
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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...
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Previous studies failed to detect c-type cytochromes in Pelobacter species despite the fact that other close relatives in the Geobacteraceae, such as Geobacter and Desulfuromonas species, have abundant c-type cytochromes. Analysis of the recently completed genome sequence of Pelobacter carbinolicus revealed 14 open reading frames that could encode c-type cytochromes. Transcripts for all but one...
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In mitochondria, two mono heme c-type cytochromes are essential electron shuttles of the respiratory chain. They are characterized by the covalent attachment of their heme C to a CXXCH motif in the apoproteins. This post-translational modification occurs in the intermembrane space compartment. Dedicated assembly pathways have evolved to achieve this chemical reaction that requires a strict redu...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96735-9