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J. Biol. Chem., Vol. 267, Issue 11, 7303-7309, Apr, 1992
MT Quinn, ML Mullen and AJ Jesaitis
Human phagocyte cytochrome b is the terminal component of the microbicidal
superoxide generating system. Although the primary structure of this
protein has been determined, little is known about the placement of the
heme prosthetic groups in this heterodimeric integral membrane protein.
Analysis of the cytochrome using lithium dodecyl sulfate-polyacrylamide gel
electrophoresis at 0 degree C followed by tetramethylbenzidine heme
staining demonstrated the presence of heme in both the 91- and 22-kDa
subunits identified by Western blot analysis using peptide specific
antisera. Exposure of cytochrome b (purified or in isolated neutrophil
plasma membranes) to Staphylococcal protease V8 or trypsin did not affect
absorbance spectra. However, such treatment resulted in degradation of both
subunits to smaller fragments, including characteristic immunoreactive
20-kDa fragments of both the large and small subunits of the cytochrome
that retained one or both of the hemes. The spectral stability to
proteolysis and size of the proteolytic heme-containing fragments generated
explains previous reports which suggested that the heme resided in the
small subunit. Our current results indicate that human neutrophil
cytochrome b is a bi-heme or possibly tri-heme molecule with at least one
heme residing in the large subunit and one shared between both subunits and
that the heme-containing regions of the cytochrome probably lie within the
membrane lipid bilayer. Such a multi-heme structure would be consistent
with an electron transfer function for this cytochrome by providing an
efficient mechanism for transferring electrons across the plasma membrane
to the extracellular surface where oxygen could be reduced to create
superoxide.
Human neutrophil cytochrome b contains multiple hemes. Evidence for heme associated with both subunits
Department of Chemistry and Biochemistry, Montana State University, Bozeman 59717.
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