Abstract
Acetobacter aceti produces two different terminal oxidases dependent on the culture conditions, shaking and static cultures. Cells grown on shaking culture contain cytochrome a1, while cytochrome o is present in cells grown on static culture. Cytochrome a1 and cytochrome o of A. aceti were compared especially with respect to the protein structure and the prosthetic groups. Cytochrome a1 exhibited lower CN sensitivity and higher affinity for O2 than cytochrome o. Both terminal oxidases consisted of four nonidentical polypeptides of which the molecular sizes were identical between both enzymes. Cytochrome a1 cross-reacted with an antibody raised against cytochrome o at the same level as cytochrome o did, and an antibody elicited against cytochrome a1 cross-reacted with both cytochrome o and cytochrome a1 at the same intensity, which indicates that both oxidases are indistinguishable immunochemically. Furthermore, almost the same peptide mapping pattern with chymotrypsin was observed in subunit I and in subunit II between both terminal oxidases, and the amino-terminal sequences in the subunit II of both oxidases were identical at least in their 10 amino acids. As for the prosthetic groups, both oxidases were shown to contain two heme-irons and one copper atom. Further, high performance liquid chromatography analysis of the heme moieties extracted from both the purified enzymes indicated that cytochrome a1 contains hemes b and a at a ratio of 1 to 1, whereas cytochrome o contains the same amounts of hemes b and o. Thus, data indicate that cytochrome a1 and cytochrome o of A. aceti are cytochrome ba and cytochrome bo ubiquinol oxidases, respectively, and that both oxidases have a closely similar protein structure and prosthetic groups, in which only heme a in the heme/copper binuclear center of cytochrome a1 is replaced by heme o in that of cytochrome o.
Highlights
Acetobacter aceti produces two different terminal Acetobacter (l), andalso divided into threegroups in terms of oxidases dependent onthe cultureconditions, shaking the terminal oxidase [4]
Cytochrome al cross-reacted with an antibody raised against cytochrome o at the same level as cytochrome o did, and an antibody elicitedagainstcytochrome al cross-reactedwithboth groups, one group including Acetobacter aceti contains only cytochrome al but theother cytochrome d [4].A. aceti is able to grow, forming a pellicle on the surface, on static culture as well as shakingculture
There is a wide variety of bacterial terminal oxidase which cytochrome o and cytochrome a, at the same intensity,can be largely classified into two groups: a ubiquinol oxidase which indicates that both oxidases are indistinguisha- and a cytochrome c oxidase
Summary
Different TerminalUbiquinol Oxidases, Cytochromea1and Cytochrome 0 , of Acetobacter aceti*. High performance liquid coli, cytochrome a a 3 of Paracoccus denitrificans, and cytochromatographyanalysis of the heme moieties ex- chrome caa of thermophilic bacterium PS3 [23] It has tracted fromboth the purified enzymes indicated that been suggested that these terminal oxidases have a similar cytochrome a,contains hemes b and a at a ratio of 1 to heme/copper binuclear center [24] and energy coupling sys-. Purification of Cytochrome a, and Cytochrome o-Cytochrome a, and cytochrome o were purified from the membranes of cells grown on shaking and static cultures, respectively, by essentially the same procedure as described in the previous paper Protein contentwas determined by the modified Lowrymethod [33]
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