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PubMed1982

On the role of factor B and oligomycin on generation and discharge of the proton gradient.

Bovine mitochondrial coupling factor B (FB) stimulates oxidative phosphorylation as well as other energy-linked reactions which are supported by ATP hydrolysis. Extraction of FB from submitochondrial particles results in a decrease in ATP-dependent proton translocation (delta pH) and binding of the voltage-sensitive dye, oxonol VI. Reconstitution of deficient particles with FB restores ATP-dependent proton translocation and oxonol binding but has little effect on oxonol binding supported by respiratory substrates.l In contrast, low levels of oligomycin stimulate oxonol binding supported by either ATP or NADH. In the case of oligomycin, the stimulatory effect is associated with a decrease in the rate of discharge of the proton gradient, but the depletion of FB or its restoration has no detectable effect on the discharge rate. The data indicate that the primary effect of FB is upon the rate of H+ translocation coupled to ATP hydrolysis, while that of low oligomycin is on the H+ permeability of the membrane.

Animals↗
PubMed1987

Isolation and structural characterization of porcine coupling factor 6 from intestinal tissues.

A polypeptide purified from an extract of thermostable, porcine intestinal peptides was found to correspond to coupling factor 6, previously known as a component of the mitochondrial oxidative phosphorylation system. The intestinal presence of this peptide offers a new source for preparation of the component in large quantities, and possibly suggests further functions of the polypeptide. Amino acid sequence analysis of this porcine form reveals it to be identical to the bovine form, except for two replacements, at position 62 (Thr in the porcine, Phe/Thr in the bovine form), and position 70 (Ala/Val). The extensive conservation suggests strict structural constraints on the functional properties of the polypeptide.

Adenosine Triphosphatases↗