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lüll Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability Sambongi Y; Uchiyama S; Kobayashi Y; Igarashi Y; Hasegawa JEur J Biochem 2002[Jul]; 269 (14): 3355-61Cytochrome c is widely distributed in bacterial species, from mesophiles to thermophiles, and is one of the best-characterized redox proteins in terms of biogenesis, folding, structure, function, and evolution. Experimental molecular biology techniques (gene cloning and expression) have become applicable to cytochrome c, enabling its engineering and manipulation. Heterologous expression systems for cytochromes c in bacteria, for use in mutagenesis studies, have been established by extensive investigation of the biological process by which the functional structure is formed. Mutagenesis and structure analyses based on comparative studies using a thermophile Hydrogenobacter thermophilus cytochrome c-552 and its mesophilic counterpart have provided substantial clues to the mechanism underlying protein stability at the amino-acid level. The molecular mechanisms underlying protein maturation, folding, and stability in bacterial cytochromes c are beginning to be understood.|Amino Acid Sequence[MESH]|Bacteria/*enzymology/genetics[MESH]|Bacterial Proteins/biosynthesis/*chemistry/physiology[MESH]|Cytochrome c Group/biosynthesis/chemistry/*physiology[MESH]|Escherichia coli Proteins/metabolism[MESH]|Hot Temperature[MESH]|Membrane Proteins/metabolism[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Oxidation-Reduction[MESH]|Oxidoreductases[MESH]|Protein Conformation[MESH]|Protein Denaturation[MESH]|Protein Disulfide-Isomerases/metabolism[MESH]|Protein Engineering[MESH]|Protein Folding[MESH]|Recombinant Fusion Proteins/biosynthesis[MESH]|Sequence Alignment[MESH]|Sequence Homology, Amino Acid[MESH]|Species Specificity[MESH] |