The subcellular loclization and properties of the ferrochelatase of etiolated barley.
The etioplast fraction prepared from dark-grown barley contained the enzyme ferrochelatase. A mitochondrial fraction prepared from the same dark-grown tissue also contained ferrochelatase. After density-gradient centrifugation an etioplast band was collected that was free from detectable mitochondrial marker enzymes and yet retained ferrochelatase activity. A membrane band that was enriched in mitochondria also contained ferrochelatase. The ferrochelatase in these two bands had different pH optima, but appeared very similar in their porphyrin specificity and their inhibition by metalloporphyrins.
D003624:Darkness; D003905:Deuteroporphyrins / Q000494:pharmacology; D003576:Electron Transport Complex IV / Q000032:analysis; D001467:Hordeum / Q000201:enzymology; D008190:Lyases / Q000032:analysis* / Q000037:antagonists & inhibitors; D008652:Mesoporphyrins / Q000494:pharmacology; D008928:Mitochondria / Q000201:enzymology; D010944:Plants / Q000201:enzymology*; D011524:Protoporphyrins / Q000494:pharmacology; D013347:Subcellular Fractions / Q000201:enzymology*
D003905:Deuteroporphyrins; D008652:Mesoporphyrins; D011524:Protoporphyrins; D003576:Electron Transport Complex IV; D008190:Lyases