Studies on ferrochelatase. The enzymic formation of haem in proplastids, chloroplasts and plant mitochondria.
1. Ferrochelatase was demonstrated in the chloroplasts and proplastids isolated from the primary leaves of beans (a dicotyledon) and oats (a monocotyledon). It was also detected in chloroplasts from etiolated bean seedlings made green by illumination before being harvested. The specific activities of the three types of bean organelles are similar, as are the specific activities of the oat proplastids and chloroplasts. 2. Chloroplasts from young spinach leaves also contain ferrochelatase; these chloroplasts were tested for their ability to form magnesium tetrapyrroles and found unable to catalyse the insertion of Mg(2+) into mesoporphyrin IX. 3. Ferrochelatase was also detected in potato tuber mitochondria. 4. Ferrochelatase activity in these plant preparations is much less stable on storage than similar preparations from bacteria and animal tissues. 5. Temperature affects the activities of spinach chloroplast ferrochelatase and rat liver ferrochelatase differently. Activity of the chloroplast enzyme increases as the temperature rises from 20.6 degrees to 26 degrees , but becomes increasingly inactivated as the temperature rises further to 38 degrees . The initial velocity of the mammalian enzyme, however, increases as the temperature rises from 25.8 degrees to 65 degrees , but the enzyme is inactivated after several minutes at 65 degrees .
D002474:Cell-Free System; D002736:Chloroplasts / Q000378:metabolism*; D002523:Edible Grain / Q000201:enzymology; D003576:Electron Transport Complex IV / Q000378:metabolism; D006418:Heme / Q000096:biosynthesis*; D007501:Iron; D008190:Lyases / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D009940:Organoids / Q000378:metabolism*; D010945:Plants, Edible / Q000201:enzymology; D013696:Temperature
D006418:Heme; D007501:Iron; D003576:Electron Transport Complex IV; D008190:Lyases