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Originally published In Press as doi:10.1074/jbc.M203820200 on June 21, 2002

J. Biol. Chem., Vol. 277, Issue 36, 33334-33337, September 6, 2002
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Vitreoscilla Hemoglobin Binds to Subunit I of Cytochrome bo Ubiquinol Oxidases*

Kyung-Won ParkDagger , Kyung-Jin KimDagger §, Andrew J. Howard, Benjamin C. Stark, and Dale A. Webster

From the Division of Biology, Department of Biological, Chemical, and Physical Sciences, Illinois Institute of Technology, Chicago, Illinois 60616

The bacterium, Vitreoscilla, can induce the synthesis of a homodimeric hemoglobin under hypoxic conditions. Expression of VHb in heterologous bacteria often enhances growth and increases yields of recombinant proteins and production of antibiotics, especially under oxygen-limiting conditions. There is evidence that VHb interacts with bacterial respiratory membranes and cytochrome bo proteoliposomes. We have examined whether there are binding sites for VHb on the cytochrome, using the yeast two-hybrid system with VHb as the bait and testing every Vitreoscilla cytochrome bo subunit as well as the soluble domains of subunits I and II. A significant interaction was observed only between VHb and intact subunit I. We further examined whether there are binding sites for VHb on cytochrome bo from Escherichia coli and Pseudomonas aeruginosa, two organisms in which stimulatory effects of VHb have been observed. Again, in both cases a significant interaction was observed only between VHb and subunit I. Because subunit I contains the binuclear center where oxygen is reduced to water, these data support the function proposed for VHb of providing oxygen directly to the terminal oxidase; it may also explain its positive effects in Vitreoscilla as well as in heterologous organisms.

* This work was supported by National Science Foundation Grants BES-9309759 and MCB-9910356 and National Institute of Standards and Technology Grant 70NANB8H0042.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Both authors contributed equally to this work.

§ To whom correspondence should be addressed: LS Bldg., BCPS Dept., 3101 S. Dearborn St., Chicago, IL 60616. Tel.: 312-567-3434; Fax: 630-252-0521; E-mail: kjkim@anl.gov.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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