Articles with "ferrochelatase" as a keyword



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Structure model of ferrochelatase from Salmonella Typhi elucidating metalation mechanism.

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Published in 2019 at "International journal of biological macromolecules"

DOI: 10.1016/j.ijbiomac.2019.01.066

Abstract: A homology model of ferrochelatase (HemH), the heme biosynthesis terminal step enzyme from Salmonella Typhi was generated to understand the mechanism of metal insertion into protoporphyrin IX for heme biosynthesis. The overall fold of membrane… read more here.

Keywords: metalation; mechanism; ferrochelatase; model ferrochelatase ... See more keywords
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Dimeric ferrochelatase bridges ABCB7 and ABCB10 homodimers in an architecturally defined molecular complex required for heme biosynthesis

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Published in 2019 at "Haematologica"

DOI: 10.3324/haematol.2018.214320

Abstract: Loss-of-function mutations in the ATP-binding cassette (ABC) transporter of the inner mitochondrial membrane, ABCB7, cause X-linked sideroblastic anemia with ataxia, a phenotype that remains largely unexplained by the proposed role of ABCB7 in exporting a… read more here.

Keywords: heme biosynthesis; ferrochelatase; abcb7 abcb10; iron ... See more keywords
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Ferrochelatase: Mapping the Intersection of Iron and Porphyrin Metabolism in the Mitochondria

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Published in 2022 at "Frontiers in Cell and Developmental Biology"

DOI: 10.3389/fcell.2022.894591

Abstract: Porphyrin and iron are ubiquitous and essential for sustaining life in virtually all living organisms. Unlike iron, which exists in many forms, porphyrin macrocycles are mostly functional as metal complexes. The iron-containing porphyrin, heme, serves… read more here.

Keywords: intersection; heme; iron; ferrochelatase ... See more keywords