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Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis
Ferrochelatase catalyzes the terminal step in heme biosynthesis, the insertion of ferrous iron into protoporphyrin to form protoheme IX. The crystal structures of human ferrochelatase both with and without protoporphyrin substrate bound have been determined previously. The substrate-free enzyme has...
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| Hlavní autoři: | , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2007
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2424199/ https://ncbi.nlm.nih.gov/pubmed/17567154 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi700151f |
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