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