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Porphyromonas gingivalis produces a functional HemH ferrochelatase important for its survival in a heme-limited environment [PDF]

open access: yesScientific Reports
Porphyromonas gingivalis, the keystone pathogen responsible for dysbiosis in the oral microbiome, the development of periodontal diseases, and the contribution to systemic comorbidities, is a heme auxotroph.
Michał Śmiga   +3 more
doaj   +2 more sources

Refolding and enzyme kinetic studies on the ferrochelatase of the cyanobacterium Synechocystis sp. PCC 6803. [PDF]

open access: yesPLoS ONE, 2013
Heme is a cofactor for proteins participating in many important cellular processes, including respiration, oxygen metabolism and oxygen binding. The key enzyme in the heme biosynthesis pathway is ferrochelatase (protohaem ferrolyase, EC 4.99.1.1), which ...
Patrik Storm   +3 more
doaj   +2 more sources

Comparison of Pyrazinamide with Isoniazid for Their Effects on the Heme Biosynthetic Pathway in Mouse Liver [PDF]

open access: yesMetabolites
Background/Objectives: Isoniazid (INH) and pyrazinamide (PZA) are first-line drugs used to treat tuberculosis (TB), but their use is generally contraindicated in patients with porphyria, a group of metabolic disorders caused by defects in the heme ...
Fu-Ying Qin   +6 more
doaj   +2 more sources

Erythropoietic protoporphyria linked to intricate double heterozygous mutations in theFECH gene: a case report and literature review [PDF]

open access: yesOrphanet Journal of Rare Diseases
Background Erythropoietic protoporphyria is an inherited disorder characterized by mutations in the FECH gene, which encodes the enzyme ferrous chelatase.
Hongli Xiong   +4 more
doaj   +2 more sources

Regulation of the expression of ferrochelatase in a murine model of diabetes mellitus type I [PDF]

open access: yesBiochemistry and Biophysics Reports
Background: Diabetes produces changes on cellular hemeprotein metabolism. The last enzyme of heme biosynthetic pathway is ferrochelatase (FECH), an enzyme that catalyzes the insertion of ferrous ion into protoporphyrin IX to produce heme. The aim of this
Leda María Oliveri   +2 more
doaj   +2 more sources

Challenges in the pathological diagnosis of erythropoietic protoporphyria: a case report [PDF]

open access: yesFrontiers in Medicine
BackgroundErythropoietic protoporphyria (EPP) is a rare autosomal recessive disorder caused by mutations in the FECH gene, leading to ferrochelatase deficiency and the accumulation of protoporphyrin in various organs.
Tingting Yang   +3 more
doaj   +2 more sources

Unraveling the potential of zinc protoporphyrin-forming lactic acid bacteria for replacing nitrite and their role in quality characteristics of Harbin dry sausage [PDF]

open access: yesFood Chemistry: X
This study evaluated the effects of zinc protoporphyrin-producing lactic acid bacteria specifically Weissella viridescens JX11, Weissella viridescens MDJ8, and Lactobacillus pentosus Q on nitrite substitution and the quality characteristics of Harbin dry
Qianhui Yang   +6 more
doaj   +2 more sources

Ferrochelatase: Mapping the Intersection of Iron and Porphyrin Metabolism in the Mitochondria

open access: yesFrontiers in Cell and Developmental Biology, 2022
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 as
Chibuike David Obi   +5 more
doaj   +1 more source

Proteomic Analysis of Ferrochelatase Interactome in Erythroid and Non-Erythroid Cells

open access: yesLife, 2023
Heme is an essential cofactor for multiple cellular processes in most organisms. In developing erythroid cells, the demand for heme synthesis is high, but is significantly lower in non-erythroid cells.
Chibuike David Obi   +4 more
doaj   +1 more source

Protoporphyrin IX Binds to Iron(II)-Loaded and to Zinc-Loaded Human Frataxin

open access: yesLife, 2023
(1) Background: Human frataxin is an iron binding protein that participates in the biogenesis of iron sulfur clusters and enhances ferrochelatase activity.
Ganeko Bernardo-Seisdedos   +4 more
doaj   +1 more source

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