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Metal ion coordination sites in ferrochelatase

期刊

COORDINATION CHEMISTRY REVIEWS
卷 460, 期 -, 页码 -

出版社

ELSEVIER SCIENCE SA
DOI: 10.1016/j.ccr.2022.214464

关键词

Enzyme; Ferrochelatase; Heme; Iron-sulfur center; Porphyrin; protoporphyrin IX

资金

  1. Florida Department of Health, Bankhead-Coley Cancer Research Program [9BC14]

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This review summarizes the scientific progress made in the last three decades on ferrochelatase and heme biosynthesis. The coordination chemistries of the ferrous iron substrate and iron-sulfur cluster in relation to the reaction mechanism and structure of mammalian ferrochelatase are discussed.
Scientific progress of the last 30 years on ferrochelatase and heme biosynthesis is summarized in this review by covering the literature related to over 100 original references. Ferrochelatase, the only chelatase in mammalian cells, catalyzes the incorporation of ferrous iron into protoporphyrin IX to give heme. Besides having a metal ion as one of its substrates, mammalian ferrochelatase itself is a metalloprotein with an iron-sulfur cofactor. The views on coordination chemistries of the ferrous iron substrate and iron-sulfur cluster are discussed in relation to the reaction mechanism and structure of ferrochelatase. (C) 2022 Elsevier B.V. All rights reserved.

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