Porcine Ferrochelatase: The Relationship between Iron-Removal Reaction and the Conversion of Heme to Zn-Protoporphyrin

Chau, Tuan Thanh; Ishigaki, Mutsumi; Kataoka, Takao; Taketani, Shigeru

doi:10.1271/bbb.100078

Cited by 30 publications

(52 citation statements)

References 30 publications

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“…However, the optimum pH value for insertion of divalent iron into protoporphyrin IX was 7.5–9.0 (Porra & Jones ) and the optimum pH value of ferrochelatase for insertion of zinc into mesoporphyrin IX was 7.5–8.0 (Chau et al . ). The optimum pH value for the formation of ZnPP in the pork liver homogenate was remarkably lower than that of ferrochelatase and is close to the pH value of meat and meat products.…”

Section: Discussionmentioning

confidence: 97%

“…On the other hand, Chau et al . () reported that the amount of Zn‐mesoporphyrin formed in the liver mitochondria was much larger than that formed in the muscle mitochondria since the amount of ferrochelatase in the muscle was small compared with the amount of hepatic enzyme. However, the optimum pH value for insertion of divalent iron into protoporphyrin IX was 7.5–9.0 (Porra & Jones ) and the optimum pH value of ferrochelatase for insertion of zinc into mesoporphyrin IX was 7.5–8.0 (Chau et al .…”

Section: Discussionmentioning

confidence: 99%

“…; Chau et al . ), the spleen might be a positive source of ZnPP. Heme is converted to unconjugated bilirubin in the spleen.…”

Section: Introductionmentioning

confidence: 99%

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A comparative study of zinc protoporphyrin IX‐forming properties of animal by‐products as sources for improving the color of meat products

Wakamatsu

Murakami

Nishimura

2014

Animal Science Journal

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The objective of this study was to obtain fundamental data for improving the color of meat products by using animal by-products. We investigated zinc protoporphyrin IX (ZnPP)-forming properties of various internal organs from pigs and chickens. ZnPP was formed in the liver, heart and kidney, whereas the porcine spleen and bile, which are involved in the metabolism of heme, did not have ZnPP-forming properties. The optimum pH values were different among the internal organs and the ZnPP-forming properties of porcine organs were better than those of chicken organs. The porcine liver showed the greatest ZnPP-forming properties among all of the internal organs investigated in this study. The optimum pH value for ZnPP formation in the liver was lower than that of skeletal muscle. Oxygen did not inhibit the formation of ZnPP in the liver, unlike in skeletal muscle. Animal by-products such as the liver have good ability for the formation of ZnPP and might be useful for improving the color of meat products.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

A comparative study of zinc protoporphyrin IX‐forming properties of animal by‐products as sources for improving the color of meat products

Wakamatsu

Murakami

Nishimura

2014

Animal Science Journal

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“…Porphyrin derivatives fluoresce in the red region at well‐defined spectral positions . Protoporphyrin IX (PPIX) belongs to the haem‐metabolic/catabolic pathways . In hepatology, some interest has been reserved for the AF of PPIX produced following the administration of its precursor 5‐aminolevulinic acid (5‐ALA), for the detection of liver tumour or bile leakage .…”

Section: Endogenous Fluorophoresmentioning

confidence: 99%

Autofluorescence‐based optical biopsy: An effective diagnostic tool in hepatology

Croce

Ferrigno

Bottiroli

et al. 2018

Liver International

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Autofluorescence emission of liver tissue depends on the presence of endogenous biomolecules able to fluoresce under suitable light excitation. Overall autofluorescence emission contains much information of diagnostic value because it is the sum of individual autofluorescence contributions from fluorophores involved in metabolism, for example, NAD(P)H, flavins, lipofuscins, retinoids, porphyrins, bilirubin and lipids, or in structural architecture, for example, fibrous proteins, in close relationship with normal, altered or diseased conditions of the liver. Since the 1950s, hepatocytes and liver have been historical models to study NAD(P)H and flavins as in situ, real-time autofluorescence biomarkers of energy metabolism and redox state. Later investigations designed to monitor organ responses to ischaemia/reperfusion were able to predict the risk of dysfunction in surgery and transplantation or support the development of procedures to ameliorate the liver outcome. Subsequently, fluorescent fatty acids, lipofuscin-like lipopigments and collagen were characterized as optical biomarkers of liver steatosis, oxidative stress damage, fibrosis and disease progression. Currently, serum AF is being investigated to improve non-invasive optical diagnosis of liver disease. Validation of endogenous fluorophores and in situ discrimination of cancerous from non-cancerous tissue belong to the few studies on liver in human subjects. These reports along with other optical techniques and the huge work performed on animal models suggest many optically based applications in hepatology. Optical diagnosis is currently offering beneficial outcomes in clinical fields ranging from the respiratory and gastrointestinal tracts, to dermatology and ophthalmology. Accordingly, this review aims to promote an effective bench to bedside transfer in hepatology.

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“…Although it has been claimed that mammalian ferrochelatase can catalyze a dechelation reaction (15), that reaction was reported to occur in vitro under non-physiologically relevant conditions at acidic pH and elevated temperature, conditions that are well outside the range where mammalian ferrochelatase is active or stable (16). Substantive evidence for metazoan and bacterial heme oxygenases exists in the literature, and in all cases the end product is a cleaved, linear tetrapyrrole, not an intact porphyrin.…”

Section: Introductionmentioning

confidence: 99%

The Escherichia coli Protein YfeX Functions as a Porphyrinogen Oxidase, Not a Heme Dechelatase

Dailey

Septer

Daugherty

et al. 2011

mBio

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The protein YfeX from Escherichia coli has been proposed to be essential for the process of iron removal from heme by carrying out a dechelation of heme without cleavage of the porphyrin macrocycle. Since this proposed reaction is unique and would represent the first instance of the biological dechelation of heme, we undertook to characterize YfeX. Our data reveal that YfeX effectively decolorizes the dyes alizarin red and Cibacron blue F3GA and has peroxidase activity with pyrogallal but not guiacol. YfeX oxidizes protoporphyrinogen to protoporphyrin in vitro. However, we were unable to detect any dechelation of heme to free porphyrin with purified YfeX or in cellular extracts of E. coli overexpressing YfeX. Additionally, Vibrio fischeri, an organism that can utilize heme as an iron source when grown under iron limitation, is able to grow with heme as the sole source of iron when its YfeX homolog is absent. Plasmid-driven expression of YfeX in V. fischeri grown with heme did not result in accumulation of protoporphyrin. We propose that YfeX is a typical dye-decolorizing peroxidase (or DyP) and not a dechelatase. The protoporphyrin reported to accumulate when YfeX is overexpressed in E. coli likely arises from the intracellular oxidation of endogenously synthesized protoporphyrinogen and not from dechelation of exogenously supplied heme. Bioinformatic analysis of bacterial YfeX homologs does not identify any connection with iron acquisition but does suggest links to anaerobic-growth-related respiratory pathways. Additionally, some genes encoding homologs of YfeX have tight association with genes encoding a bacterial cytoplasmic encapsulating protein.

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Porcine Ferrochelatase: The Relationship between Iron-Removal Reaction and the Conversion of Heme to Zn-Protoporphyrin

Cited by 30 publications

References 30 publications

A comparative study of zinc protoporphyrin IX‐forming properties of animal by‐products as sources for improving the color of meat products

A comparative study of zinc protoporphyrin IX‐forming properties of animal by‐products as sources for improving the color of meat products

Autofluorescence‐based optical biopsy: An effective diagnostic tool in hepatology

The Escherichia coli Protein YfeX Functions as a Porphyrinogen Oxidase, Not a Heme Dechelatase

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