Functional and Structural Comparisons between Prokaryotic and Enkaryotic aa_3-Type Cytochrome c Oxidases from an Evolutionary Point of View

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概要

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• The specificities for cytochrome c of the aa_3-type cytochrome c oxidase were studied with enzymes derived from Thiobacillus novellus, Nitrobacter agilis, Paracoccus denitnficans and the cow in reaction with the cytochromes c from 5 prokaryotes and 7 eukaryotes. The T. novellus enzyme reacted most rapidly with the cytochromes c of Candida krusei, tuna and bonito as well as T. novellus cytochrome c; the specificity for cytochrome c of the N. agilis enzyme was similar to that of the T. novellus enzyme. The bovine enzyme reacted rapidly with all the eukaryotic cytochromes c tested. The P. denitnficans enzyme showed a specificity similar to that of the bovine enzyme, except that it reacted rapidly with P. denitnficans cytochrome c, while the bovine enzyme reacted with it very poorly. All four kinds of enzymes showed an extremely limited reaction with Pseudomonas aeruginosa cytochrome c. The amino acid composition of subunit I of the N. agilis enzyme resembled that of the bovine enzyme, while the compositions of their subunits 11 were different. On the basis of these results, an evolutionary relationship between bacterial and eukaryotic enzymes was discussed.

• 日本植物生理学会の論文

著者

• Yamanaka Tateo

  Department Of Biology Faculty Of Science Osaka University

• Fukumori Yoshihiro

  Department Of Biology Faculty Of Science Kanazawa University

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