Fumarate Reductase in the Control of Heme Biosynthesis
- 11 March 1966
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 151 (3715) , 1228-1229
- https://doi.org/10.1126/science.151.3715.1228
Abstract
A drug-induced stimulation of heme biosynthesis in mouse liver was accompanied by altered fumarate metabolism. In liver homogenate, fumarate-1,4-C 14 was incorporated, via succinate and succinyl coenzyme A, into heme at an accelerated rate. This pathway of fumarate utilization was inhibited by acetoacetate but not by β-hydroxybutyrate. Fumarate reduction to succinate required reduced nicotinamide adenine dinucleotide. The enzyme fumarate reductase is suggested as a link between terminal oxidation and cellular control of the heme biosynthetic pathway.Keywords
This publication has 6 references indexed in Scilit:
- Magnesium accumulation by liver mitochondria in experimental porphyriaBiochimica et Biophysica Acta (BBA) - General Subjects, 1965
- The role of succinyl-CoA synthetase in the control of heme biosynthesisBiochimica et Biophysica Acta (BBA) - General Subjects, 1965
- Terminal Oxidation in the Regulation of Heme BiosynthesisScience, 1963
- Oxidative metabolism of tissue culture cells in the presence of porphyria-inducing drugsArchives of Biochemistry and Biophysics, 1963
- Relation of barbiturate structure to DPNH oxidase inhibitionArchives of Biochemistry and Biophysics, 1962
- THE MECHANISM OF PORPHYRIN FORMATIONPublished by Elsevier ,1952