Cytochromes c of Nitrobacter winogradskyi and Thiobacillus novellus: structure, function and evolution.
The amino acid sequences of Thiobacillus novellus and Nitrobacter winogradskyi cytochromes c have been compared with those of cytochromes c from several other organisms. The two bacterial cytochromes resemble eukaryotic cytochromes c; 49 amino-acid residues are identical between T. novellus and horse cytochromes c, and 50 residues identical between N. winogradskyi and horse cytochromes c. However, their reactivity with cow cytochrome c oxidase is about 80% lower than the reactivity of eukaryotic cytochromes c with the cow mitochondrial oxidase, while they react with yeast cytochrome c peroxidase as rapidly as eukaryotic cytochromes c. The numbers of identical amino-acid residues between T. novellus and animal cytochromes c are 45-53 and those between N. winogradskyi and animal cytochromes c 47-53, while those between the two bacterial cytochromes and yeast and protozoan cytochromes c are around 40. Thus, N. winogradskyi and T. novellus cytochromes c are more similar to animal cytochromes c than to yeast and protozoan cytochromes c on the basis of the amino-acid sequence.
Yamanaka
T
T
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Nagano
T
T
Shoji
K
K
Fukumori
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002417:Cattle; D003574:Cytochrome c Group / Q000737:chemistry / Q000235:genetics* / Q000502:physiology; D006736:Horses; D008239:Lysine; D008969:Molecular Sequence Data; D009576:Nitrobacter / Q000201:enzymology*; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship; D013855:Thiobacillus / Q000201:enzymology*
D003574:Cytochrome c Group; D008239:Lysine