Results 101 to 110 of about 4,768 (212)

Porphyrinogenic activity and ferrochelatase-inhibitory activity of sydnones in chick embryo liver cells

, 1986
3-[2-(2,4,6-Trimethylphenyl)thioethyl]-4-methylsydnone was shown to be a potent porphyrinogenic agent in chick embryo liver cells. The accumulation of protoporphyrin IX was consistent with the finding that ferrochelatase activity was inhibited.
P.R.Ortiz de Montellano, de Montellano, P.R.Ortiz, L.A. Grab, Sutherland, E.P., Marks, G.S., Grab, L.A., G.S. Marks, E.P. Sutherland   +7 more
core   +1 more source

Metal Binding to Saccharomyces cerevisiae Ferrochelatase

, 2002
Ferrochelatase is the terminal enzyme in the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into protoporphyrin IX to produce protoheme IX.
Al-Karadaghi, Salam, Lecerof, David,, Lecerof, David, Labbe-Bois, Rosine, Karlberg, Tobias,, Hansson, Mats,, Lund University., Silvergren, Germund, Hansson, Mats, Gora, Monika, Karlberg, Tobias, Al-Karadaghi, Salam,   +11 more
core   +1 more source

PufQ regulates porphyrin flux at the haem/bacteriochlorophyll branchpoint of tetrapyrrole biosynthesis via interactions with ferrochelatase [PDF]

, 2017
Facultative phototrophs such as Rhodobacter sphaeroides can switch between heterotrophic and photosynthetic growth. This transition is governed by oxygen tension and involves the large-scale production of bacteriochlorophyll, which shares a biosynthetic ...
Jackson, P.J., Chidgey, J.W., Mark J. Dickman, Dickman, M.J., Jack W. Chidgey, Philip J. Jackson, C. Neil Hunter, Hunter, C.N.   +7 more
core   +1 more source

Characterization of the iron-binding site in mammalian ferrochelatase by kinetic and Mössbauer methods

, 1995
NIGMS NIH HHS (GM47295)All organisms utilize ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) to catalyze the terminal step of the heme biosynthetic pathway, which involves the insertion of ferrous ion into protoporphyrin IX.
Lloyd, Steven G., Huynh, Boi Hanh, Moura, José J. G., Moura, Isabel, Forbes, William S., Ferreira, Glória C., Franco, Ricardo   +6 more
core   +1 more source

Molecular characterisation of erythropoietic protoporphyria in South Africa

, 2006
Includes bibliographical ...
Parker, Michelle
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Role of Bacterioferritin & Ferritin in M. tuberculosis Pathogenesis and Drug Resistance: A Future Perspective by Interactomic Approach

Frontiers in Cellular and Infection Microbiology, 2017
Tuberculosis is caused by Mycobacterium tuberculosis, one of the most successful and deadliest human pathogen. Aminoglycosides resistance leads to emergence of extremely drug resistant strains of M. tuberculosis.
Divakar Sharma, Deepa Bisht
doaj   +1 more source

Ferrochelatase of lettuce chloroplasts [PDF]

Biochemical Journal, 1968
R F, King, E R, Page
openaire   +2 more sources

Heme biosynthesis: structure-activity studies of murine ferrochelatase

, 2006
Ferrochelatase catalyzes the terminal step of heme biosynthesis by inserting ferrous iron into protoporphyrin IX. The current study is aimed at understanding the structural basis of porphyrin binding and distortion in ferrochelatase-catalyzed reaction by
Shi, Zhen
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Erythropoietic protoporphyria in the house mouse. A recessive inherited ferrochelatase deficiency with anemia, photosensitivity, and liver disease.

, 1991
International audienceA viable autosomal recessive mutation (named fch, or ferrochelatase deficiency) causing jaundice and anemia in mice arose in a mutagenesis experiment using ethylnitrosourea.
Rouyer-Fessard, P, J L Guénet, P Rouyer-Fessard, Guénet, J, L, Y Beuzard, Deybach, J, C, V Da Silva, Y Nordmann, X Montagutelli, Tutois, S, H Jouault, Montagutelli, X., Beuzard, Y, Jouault, J, Jouault, H, S Tutois, J C Deybach, da Silva, V, K Leroy-Viard, Leroy-Viard, K, Nordmann, Y   +20 more
core   +1 more source

Iron in Haem Biosynthesis. Structural Studies of Ferrochelatase and Frataxin.

, 2006
Ferrochelatase catalyses the synthesis of heme by inserting Fe(II) into protoporphyrin IX. The structure of ferrochelatase from yeast has been determined (2.4 Å).
Karlberg, Tobias
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