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. 1968 May;95(5):1774–1778. doi: 10.1128/jb.95.5.1774-1778.1968

Identification of Propionate as an Endogenous CO2 Acceptor in Rhodospirillum rubrum and Properties of Purified Propionyl-Coenzyme A Carboxylase

I Olsen a,1, J M Merrick b
PMCID: PMC252211  PMID: 5650084

Abstract

A heat-stable endogenous CO2 acceptor has been found in extracts of Rhodospirillum rubrum grown photoheterotrophically on acetate. Evidence is presented which suggests that this factor is propionic acid. Thus, paper and gas chromatographic analyses have indicated that propionic acid is present in boiled extracts prepared from R. rubrum cells. The products of 14CO2 fixation obtained with either the boiled extract or propionic acid as the CO2 acceptor were identical and were identified as methylmalonic acid and succinic acid by paper chromatography. The enzyme which catalyzes the carboxylation of propionyl-coenzyme A (propionyl-CoA carboxylase) was purified from R. rubrum cells grown on acetate and its properties were studied. The enzyme is similar to propionyl-CoA carboxylases isolated from mammalian sources.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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