Composition of the heme centers in chromaffin granule cytochrome b(561).
Electron paramagnetic resonance and circular dichroism spectra of cytochrome b(561) from chromaffin granule membranes indicated a 2:1 stoichiometry of high- and low-potential hemes. Recombinant bovine cytochrome b(561) expressed in a baculovirus system retained native spectroscopic characteristics and represents a promising model for further study.
Kamensky
Yury
Y
Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005, USA. yuryk@bioc.rice.edu
Kulmacz
Richard J
RJ
Palmer
Graham
G
D000818:Animals; D001205:Ascorbic Acid / Q000378:metabolism; D016367:Baculoviridae / Q000378:metabolism; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D019439:Chromaffin Cells / Q000378:metabolism*; D002942:Circular Dichroism; D003573:Cytochrome b Group / Q000737:chemistry*; D004299:Dopamine beta-Hydroxylase / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D005982:Glutathione Transferase / Q000378:metabolism; D006418:Heme / Q000737:chemistry*; D015151:Immunoblotting; D008954:Models, Biological; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013053:Spectrophotometry
D003573:Cytochrome b Group; D011993:Recombinant Fusion Proteins; C023646:cytochrome b561; D006418:Heme; D004299:Dopamine beta-Hydroxylase; D005982:Glutathione Transferase; D001205:Ascorbic Acid