Results 121 to 130 of about 4,023 (167)

Organelle regulation of ferroptosis after intracerebral hemorrhage. [PDF]

Redox Biol
Zhou N, Du Y, Wang Y, Zhao X, Ju Y.
europepmc   +1 more source

Enhanced heme production in industrial Saccharomyces cerevisiae through metabolic engineering. [PDF]

NPJ Sci Food
Lee HJ, Lee TG, Cho C, Jeon GB, Oh S, Kim SK.   +5 more
europepmc   +1 more source

Updates to gene-disease classifications and inheritance patterns for porphyrias. [PDF]

Mol Genet Metab
Reeves EB, Hankey W, Clair PS, Goldstein JL, Wilke MVMB, Feigenbaum A, Hung C, Spector E, Craigen WJ.   +8 more
europepmc   +1 more source

Redox status regulates eggshell color by modulating protoporphyrin IX biosynthesis via the SIRT1/PGC-1α/ALAS1 axis in brown-shelled hens. [PDF]

J Anim Sci Biotechnol
Fu Y, Lu M, Liu D, Wang J, Zhang H, Qi G, Wang J.   +6 more
europepmc   +1 more source

Real-world assessment of the patient profile, clinical characteristics, treatment patterns, and outcomes associated with erythropoietic and X-linked protoporphyria. [PDF]

J Dermatol
Silver SM, Houghton K, Hitchens A, Ansquer VD, Ciepielewska M.   +4 more
europepmc   +1 more source

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A simple ferrochelatase assay

Biochimie, 1981
Jean-Michel Camadro, P Labbé, J M Camadro   +2 more
exaly   +3 more sources

Interaction of free porphyrins and metalloporphyrins with mouse ferrochelatase. A model for the active site of ferrochelatase

BBA - Proteins and Proteomics, 1989
The ability of purified mouse ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1) to bind and catalytically utilize a variety of porphyrins has been examined. In all, the kd, Km or Ki values for eleven different porphyrins, the Ki values for four metalloporphyrins and the kd values for two metalloporphyrins were determined.
Harry A Dailey
exaly   +3 more sources

Saccharomyces cerevisiae Ferrochelatase Forms a Homodimer

Archives of Biochemistry and Biophysics, 2002
Ferrochelatase, the last enzyme of the heme biosynthetic pathway, has for years been considered to be active as a monomer. The crystal structure of Bacillus subtilis ferrochelatase confirmed its monomeric structure. However, animal ferrochelatase was found to form a functional dimer.
Monika Gora, Ewa Grzybowska, Danuta Plochocka   +2 more
exaly   +3 more sources

Structure and function of ferrochelatase

Journal of Bioenergetics and Biomembranes, 1995
Ferrochelatase is the terminal enzyme of the heme biosynthetic pathway in all cells. It catalyzes the insertion of ferrous iron into protoporphyrin IX, yielding heme. In eukaryotic cells, ferrochelatase is a mitochondrial inner membrane-associated protein with the active site facing the matrix. Decreased values of ferrochelatase activity in all tissues
G C, Ferreira, R, Franco, S G, Lloyd, I, Moura, J J, Moura, B H, Huynh   +5 more
openaire   +2 more sources

Properties of the Cobaltochelatase and the Ferrochelatase

Enzyme, 2017
The formation of cobaltomesoporphyrin and ferromesoporphyrin in the presence of appropriate chelatases has been studied. The K(m) value for mesoporphyrin differs for the two activities, although the optimum pH value is 8.1 for both. At high cobalt concentrations a slight non-enzymatic reaction occurs which is not seen with ferrous salts.
E T, Canepa, E B, Llambias
openaire   +2 more sources