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Journal of Biochemistry Advance Access published online on May 4, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp067
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Biochemical and spectroscopic properties of cyanide-insensitive quinol oxidase from Gluconobacter oxydans

Tatsushi Mogi1,2,*, Yoshitaka Ano3, Tomoko Nakatsuka3, Hirohide Toyama3,§, Atsushi Muroi4, Hideto Miyoshi4, Catharina T. Migita3, Hideaki Ui5, Kazuro Shiomi5, Satoshi Omura5, Kiyoshi Kita1 and Kazunobu Matsushita3,*

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; 3Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753-8515; 4Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502; 5Kitasato Institute for Life Sciences and Graduate School of Infection Control Sciences, Kitasato University, Minato-ku, Tokyo 108-8641, Japan

*To whom correspondence addressed. Tel: +81-3-5841-8202, Fax: +81-3-5841-3444, E-mail: tmogi{at}m.u-tokyo.ac.jp (T. Mogi). Tel: +81-83-933-5858, Fax: +81-83-933-5859, E-mail: kazunobu{at}agr.yamaguchi-u.ac.jp (K. Matsushita)

Received February 18, 2009; Accepted April 9, 2009


  Abstract

Cyanide-insensitive quinol oxidase (CioAB), a relative of cytochrome bd, has no spectroscopic features of hemes b595 and d in the wild-type bacteria and is difficult to purify for detailed characterization. Here we studied enzymatic and spectroscopic properties of CioAB from the acetic acid bacterium Gluconobacter oxydans. G. oxydans CioAB showed the Km value for ubiquinol-1 comparable to that of Escherichia coli cytochrome bd but it was more resistant to KCN and quinone-analog inhibitors except piericidin A and LL-Z1272{gamma}. We obtained the spectroscopic evidence for the presence of hemes b595 and d. Heme b595 showed the {alpha} peak at 587 nm in the reduced state and a rhombic high-spin signal at g = 6.3 and 5.5 in the air-oxidized state. Heme d showed the {alpha} peak at 626 and 644 nm in the reduced and air-oxidized state, respectively, and an axial high-spin signal at g = 6.0 and low-spin signals at g = 2.63, 2.37 and 2.32. We found also a broad low-spin signal at g = 3.2, attributable to heme b558. Further, we identified the presence of heme D by mass spectrometry. In conclusion, CioAB binds all three heme species present in cytochrome bd quinol oxidase.

Key Words: Acetic acid bacteria, Cyanide-insensitive oxidase, Cytochrome bd, Heme d, Quinol oxidase

§Present address: Department of Bioscience and Biotechnology, Faculty of Agriculture, University of the Ryukyus, Okinawa 903-0213, Japan


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