Reference on EC 4.99.1.9 - coproporphyrin ferrochelatase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hansson, M.; Hederstedt, L.
Purification and characterisation of a water-soluble ferrochelatase from Bacillus subtilis
Eur. J. Biochem.
220
201-208
1994
Bacillus subtilis
Hansson, M.D.; Karlberg, T.; Rahardja, M.A.; Al-Karadaghi, S.; Hansson, M.
Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX
Biochemistry
46
87-94
2007
Bacillus subtilis (P32396), Bacillus subtilis 168 (P32396)
Xu, K.; Delling, J.; Elliott, T.
The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation
J. Bacteriol.
174
3953-3963
1992
Salmonella enterica subsp. enterica serovar Typhimurium
Hansson, M.; Hederstedt, L.
Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes
J. Bacteriol.
174
8081-8093
1992
Bacillus subtilis (P32396), Bacillus subtilis 168 (P32396)
Dailey, H.A.; Gerdes, S.; Dailey, T.A.; Burch, J.S.; Phillips, J.D.
Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin
Proc. Natl. Acad. Sci. USA
112
2210-2215
2015
Bacillus subtilis, Cutibacterium acnes, Mycobacterium tuberculosis
Al-Karadaghi, S.; Hansson, M.; Nikonov, S.; Jonsson, B.; Hederstedt, L.
Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis
Structure
5
1501-1510
1997
Bacillus subtilis, Bacillus subtilis 168
Hofbauer, S.; Helm, J.; Obinger, C.; Djinovic-Carugo, K.; Furtmueller, P.G.
Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase
FEBS J.
287
2779-2796
2020
Listeria monocytogenes (A0A5D5VUB4)
Gabler, T.; Sebastiani, F.; Helm, J.; Dali, A.; Obinger, C.; Furtmueller, P.G.; Smulevich, G.; Hofbauer, S.
Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propionate groups
FEBS J.
289
1680-1699
2022
Listeria monocytogenes (A0A5D5VUB4)
Dali, A.; Gabler, T.; Sebastiani, F.; Destinger, A.; Furtmueller, P.G.; Pfanzagl, V.; Becucci, M.; Smulevich, G.; Hofbauer, S.
Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III propionate interactions and porphyrin core deformation
Protein Sci.
32
e4534
2023
Listeria monocytogenes (A0A5D5VUB4)
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