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J Biol Chem, Vol. 274, Issue 46, 32810-32817, November 12, 1999

A Cytochrome bb'-type Quinol Oxidase in Bacillus subtilis Strain 168

Natalia Azarkina, Sergey Siletsky, Vitaliy Borisov, Claes von Wachenfeldt^§, Lars Hederstedt^§, and Alexander A. Konstantinov

From the  A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia and the ^§ Department of Microbiology, Lund University, Sölvegatan 12, SE-223 62 Lund, Sweden

The aerobic respiratory system of Bacillus subtilis 168 is known to contain three terminal oxidases: cytochrome caa₃, which is a cytochrome c oxidase, and cytochrome aa₃ and bd, which are quinol oxidases. The presence of a possible fourth oxidase in the bacterium was investigated using a constructed mutant, LUH27, that lacks the aa₃ and caa₃ terminal oxidases and is also deficient in succinate:menaquinone oxidoreductase. The cytochrome bd content of LUH27 can be varied by using different growth conditions. LUH27 membranes virtually devoid of cytochrome bd respired with NADH or exogenous quinol as actively as preparations containing 0.4 nmol of cytochrome bd/mg of protein but were more sensitive to cyanide and aurachin D. The reduced minus oxidized difference spectra of the bd-deficient membranes as well as absorption changes induced by CO and cyanide indicated the presence of a "cytochrome o"-like component; however, the membranes did not contain heme O. The results provide strong evidence for the presence of a terminal oxidase of the bb' type in B. subtilis. The enzyme does not pump protons and combines with CO much faster than typical heme-copper oxidases; in these respects, it resembles a cytochrome bd rather than members of the heme-copper oxidase superfamily. The genome sequence of B. subtilis 168 contains gene clusters for four respiratory oxidases. Two of these clusters, cta and qox, are deleted in LUH27. The remaining two, cydAB and ythAB, encode the identified cytochrome bd and a putative second cytochrome bd, respectively. Deletion of ythAB in strain LUH27 or the presence of the yth genes on plasmid did not affect the expression of the bb' oxidase. It is concluded that the novel bb'-type oxidase probably is cytochrome bd encoded by the cyd locus but with heme D being substituted by high spin heme B at the oxygen reactive site, i.e. cytochrome b₅₅₈b₅₉₅b'.

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