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³²P-Labeling of Mitochondrial Protein and Lipid Fractions and Their Relation to Oxidative Phosphorylation

From the ¹ From the Department of Chemistry and Molecular Biology Institute, University of California, Los Angeles, California 90024

Evidence is presented that phosphorylated proteins or lipids containing phosphohistidine, phosphoserine, or other phosphoryl groups stable to phenol extraction at acidic, near neutral, or alkaline pH do not serve as intermediates in the formation of adenosine triphosphate by oxidative phosphorylation in mitochondrial particles. Suggestions of phosphoproteins as intermediates are thus considered to be tenuous.

It has been shown that an unidentified, apparently protein-bound, and very labile phosphate fraction rapidly formed from ³²P_i in mitochondria and particles probably represents a specifically occluded P_i and not a labile phosphoryl derivative. This P_i does not appear to be at or near the site of oxidative phosphorylation.

In intact mitochondria, bound phosphohistidine is labeled much more rapidly and initially to a greater extent than phosphoserine or lipid phosphate fractions, and independently from the labeling of these fractions. Phosphohistidine may be labeled directly from P_i, but labeling of the phosphoserine and lipid phosphate fractions by ³²P_i appears to occur only via intermediate formation of AT³²P. Transphosphorylation among the various fractions does not occur under conditions tested. Most of the lipid phosphate labeling from AT³²P occurs near the mitochondrial surface in an atractyloside-insensitive locus.

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