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Journal of Biochemistry Advance Access originally published online on January 2, 2009
Journal of Biochemistry 2009 145(3):395-401; doi:10.1093/jb/mvn179
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© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Properties of Cytochrome bd Plastoquinol Oxidase from the Cyanobacterium Synechocystis sp. PCC 6803

Tatsushi Mogi1,2,* and Hideto Miyoshi3

1Department of Biomedical Chemistry, Graduate School of Medicine, the University of Tokyo, Bunkyo-ku, Tokyo 113-0033; 2ATP System Project, ERATO, JST, Nagatsuta, Yokohama, 226-0026; and 3Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan

*To whom correspondence addressed. Tel: +81-3-5841-8202, Fax: +81-3-5841-3444, E-mail: tmogi{at}m.u-tokyo.ac.jp

Received October 9, 2008; Accepted December 15, 2008


  Abstract

In the aerobic respiratory chain of the cyanobacterium Synechocystis sp. PCC 6803, cytochrome c oxidase serves as a major terminal oxidase while cyanide-resistant cytochrome bd serves as an alternative oxidase and evades the over-reduction of the plastoquinone pool under stress conditions. Here we expressed Synechocystis cytochrome bd in Escherichia coli and characterized enzymatic and spectroscopic properties. Cyanobacterial cytochrome bd showed the higher activity with ubiquinols than with decyl-plastoquinol and Km values for quinols were 2-fold smaller than those of E. coli cytochrome bd (CydAB). The dioxygen reduction site was resistant to cyanide as in E. coli oxidase while the quinol oxidation site was more sensitive to antimycin A and quinolone inhibitors. Spectroscopic analysis showed the presence of the haem b595-d binuclear centre but the sequence analysis indicates that cyanobacterial cytochrome bd is structurally related to cyanide-insensitive oxidase (CioAB), which does not show typical spectral changes upon reduction and ligand binding. Our data indicate that cyanobacterial cytochrome bd has unique enzymatic and structural properties and we hope that our findings will help our understanding the role and properties of CydAB and CioAB quinol oxidases in other bacterial species.

Key Words: absorption spectra, cyanobacteria, cytochrome bd, kinetics, plastoquinol oxidase

Abbreviations: HQNO, 2-heptyl-4-hydroxyquinoline-N-oxide; IC50, the 50% inhibitory concentration


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