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Originally published In Press as doi:10.1074/jbc.M009808200 on April 30, 2001

J. Biol. Chem., Vol. 276, Issue 27, 24781-24789, July 6, 2001
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Vitreoscilla Hemoglobin
INTRACELLULAR LOCALIZATION AND BINDING TO MEMBRANES*

RamandeepDagger §, Kwang Woo Hwang§, Manoj RajeDagger , Kyung-Jin Kim, Benjamin C. Stark, Kanak L. DikshitDagger ||, and Dale A. Webster||

From the Dagger  Institute of Microbial Technology, Sector 39, Chandigarh 160014, India, and the  Department of Biological, Chemical, and Physical Sciences, Illinois Institute of Technology, Chicago, Illinois 60616

The obligate aerobic bacterium, Vitreoscilla, synthesizes elevated quantities of a homodimeric hemoglobin (VHb) under hypoxic growth conditions. Expression of VHb in heterologous hosts often enhances growth and product formation. A role in facilitating oxygen transfer to the respiratory membranes is one explanation of its cellular function. Immunogold labeling of VHb in both Vitreoscilla and recombinant Escherichia coli bearing the VHb gene clearly indicated that VHb has a cytoplasmic (not periplasmic) localization and is concentrated near the periphery of the cytosolic face of the cell membrane. OmpA signal-peptide VHb fusions were transported into the periplasm in E. coli, but this did not confer any additional growth advantage. The interaction of VHb with respiratory membranes was also studied. The Kd values for the binding of VHb to Vitreoscilla and E. coli cell membranes were ~5-6 µM, a 4-8-fold higher affinity than those of horse myoglobin and hemoglobin for these same membranes. VHb stimulated the ubiquinol-1 oxidase activity of inverted Vitreoscilla membranes by 68%. The inclusion of Vitreoscilla cytochrome bo in proteoliposomes led to 2.4- and 6-fold increases in VHb binding affinity and binding site number, respectively, relative to control liposomes, suggesting a direct interaction between VHb and cytochrome bo.

* This work was supported by NSF, National Institutes of Health Department of Science and Technology United States-India Cooperative Grant INT-9811595, NSF, National Institutes of Health Grant MCB-9910356, and a grant from the Department of Biotechnology, Government of India.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.

|| To whom correspondence may be addressed. Fax: 312-567-3494; E-mail: dale.webster@iit.edu; kanak@imtech.res.in.

§ Both authors contributed equally to this work. Submitted in partial fulfillment of the requirements for the Ph.D. degree at the Institute of Microbial Technology (for R.) and at the Illinois Institute of Technology (for K. W. H.).

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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