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. 1968 Jun;108(2):343–348. doi: 10.1042/bj1080343

Studies on ferrochelatase. The enzymic formation of haem in proplastids, chloroplasts and plant mitochondria

R J Porra 1, June Lascelles 1,*
PMCID: PMC1198814  PMID: 4298995

Abstract

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 Mg2+ 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° to 26°, but becomes increasingly inactivated as the temperature rises further to 38°. The initial velocity of the mammalian enzyme, however, increases as the temperature rises from 25·8° to 65°, but the enzyme is inactivated after several minutes at 65°.

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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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