Results 111 to 120 of about 5,252 (212)

Metallation of the transition-state inhibitor N-methyl mesoporphyrin by ferrochelatase: Implications for the catalytic reaction mechanism

, 2005
Insertion of metals into various tetrapyrroles is catalysed by a group of enzymes called chelatases, e.g. nickel, cobalt, magnesium and ferrochelatase.
Hansson, Mattias, Al-Karadaghi, Salam, Reimann, Curt, Shipovskov, Stepan, Fodje, Michel, Hansson, Mats, Ferreira, Gloria C, Karlberg, Tobias, Fodje, Michel,, Hansson, Mattias,, Hansson, Mats,, Al-Karadaghi, Salam,, Reimann, Curt,, Karlberg, Tobias,, Lund University., Shipovskov, Stepan,   +15 more
core   +1 more source

Molecular defects in ferrochelatase in patients with protoporphyria requiring liver transplantation. [PDF]

, 1998
Protoporphyria is a genetic disorder in which a deficiency of mitochondrial ferrochelatase activity causes accumulation of protoporphyrin that produces severe liver damage in some patients.
Bruzzone, C, Zhu, L, S Magness, Scarlett, Y, Magness, S, Brenner, D, L Zhu, J Bloomer, Y Scarlett, Bloomer, J, C Bruzzone, D Brenner   +11 more
core   +1 more source

Ferrochelatase of lettuce chloroplasts [PDF]

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

Direct Spectroscopic Ferrochelatase Assay

Ferrochelatases (E.C. 4.99.1.1) catalyze the insertion of ferrous iron into either protoporphyrin IX to make protoheme IX or coproporphyrin III to make coproheme III. Ferrochelatase activity in extracts or purified protein can be measured via several assays.
Dailey, Harry A., Medlock, Amy E.
openaire   +2 more sources

Analysis of ferrochelatase expression during hematopoietic development of embryonic stem cells

, 2000
Ferrochelatase, the last enzyme in the heme pathway, chelates protoporphyrin IX and iron to form heme and is mutated in protoporphyria. The ferrochelatase gene is expressed in all tissues at low levels to provide heme for essential heme-containing ...
Magness, Scott T., Tugores, Antonio, Brenner, David A.   +2 more
core   +1 more source

Crystallographic studies on porphyrin metallation by ferrochelatase.

, 2002
Ferrochelatase catalyses the terminal step in heme biosynthesis by inserting a ferrous ion into protoporphyrin IX. The reaction mechanism has in this thesis been studied by mainly crystallographic methods.
Lecerof, David
core  

Mitochondrial Heme Synthesis Enzymes as Therapeutic Targets in Vascular Diseases

Frontiers in Pharmacology, 2020
Trupti Shetty, Trupti Shetty, Timothy W. Corson, Timothy W. Corson, Timothy W. Corson   +4 more
doaj   +1 more source

Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX

, 2007
Ferrochelatase catalyzes the terminal step in the heme biosynthetic pathway, i.e., the incorporation of Fe(II) into protoporphyrin IX. Various biochemical and biophysical methods have been used to probe the enzyme for metal binding residues and the ...
Hansson, Mattias, Al-Karadaghi, Salam, Rahardja, Muhammad Arys, Karlberg, Tobias,, Hansson, Mattias,, Hansson, Mats,, Lund University., Hansson, Mats, Karlberg, Tobias, Al-Karadaghi, Salam,   +9 more
core   +1 more source

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
core  

Inactivation of cytochrome P450 and inhibition of ferrochelatase by analogues of 3,5-diethoxycarbonyl-l,4-dihydro-2,4,6-trimethylpyridine with 4-nonyl and 4-dodecyl substituents

, 1992
Cytochrome P450- and heme-destructive effects of the 4-nonyl and 4-dodecyl analogues of 3,5-diethoxycarbonyl-1,4-dihydro-2,4,6-trimethylpyridine (DDC) were determined using hepatic microsomal preparations obtained from untreated, β-naphthoflavone ...
R. A. Whitney, S. M. Kimmett, D. S. Riddick, S. A. McCluskey, J. E. Mackie, G. S. Marks   +5 more
core   +1 more source