Reference on EC 1.3.98.5 - hydrogen peroxide-dependent heme synthase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Celis, A.I.; Streit, B.R.; Moraski, G.C.; Kant, R.; Lash, T.D.; Lukat-Rodgers, G.S.; Rodgers, K.R.; DuBois, J.L.
Unusual peroxide-dependent, heme-transforming reaction catalyzed by HemQ
Biochemistry
54
4022-4032
2015
Staphylococcus aureus, Staphylococcus aureus (A0A0S3DY11)
Hofbauer, S.; Mlynek, G.; Milazzo, L.; Puehringer, D.; Maresch, D.; Schaffner, I.; Furtmueller, P.G.; Smulevich, G.; Djinovic-Carugo, K.; Obinger, C.
Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies
FEBS J.
283
4386-4401
2016
Listeria monocytogenes (Q8Y5F1), Listeria monocytogenes serotype 1/2a (Q8Y5F1), Listeria monocytogenes ATCC BAA-679 (Q8Y5F1), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y5F1)
Celis, A.I.; Gauss, G.H.; Streit, B.R.; Shisler, K.; Moraski, G.C.; Rodgers, K.R.; Lukat-Rodgers, G.S.; Peters, J.W.; DuBois, J.L.
A structure-based mechanism for oxidative decarboxylation reactions mediated by amino acids and heme propionates in coproheme decarboxylase (HemQ)
J. Am. Chem. Soc.
139
1900-1911
2017
Geobacillus stearothermophilus (A0A0K2H9D8), Geobacillus stearothermophilus 10 (A0A0K2H9D8)
Dailey, T.A.; Boynton, T.O.; Albetel, A.N.; Gerdes, S.; Johnson, M.K.; Dailey, H.A.
Discovery and characterization of HemQ an essential heme biosynthetic pathway component
J. Biol. Chem.
285
25978-25986
2010
Bacillus subtilis, Mycobacterium tuberculosis, Cutibacterium acnes, Streptomyces coelicolor
Hofbauer, S.; Hagmueller, A.; Schaffner, I.; Mlynek, G.; Krutzler, M.; Stadlmayr, G.; Pirker, K.; Obinger, C.; Daims, H.; Djinovic-Carugo, K.; Furtmueller, P.
Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes
Arch. Biochem. Biophys.
574
36-48
2015
Listeria monocytogenes serotype 1/2a (Q8Y5F1), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y5F1)
Hobbs, C.; Dailey, H.; Shepherd, M.
The HemQ coprohaem decarboxylase generates reactive oxygen species Implications for the evolution of classical haem biosynthesis
Biochem. J.
473
3997-4009
2016
Staphylococcus aureus (A0A0S3DY11)
Milazzo, L.; Hofbauer, S.; Howes, B.D.; Gabler, T.; Furtmueller, P.G.; Obinger, C.; Smulevich, G.
Insights into the active site of coproheme decarboxylase from Listeria monocytogenes
Biochemistry
57
2044-2057
2018
Listeria monocytogenes serotype 1/2a (Q8Y5F1), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y5F1)
Milazzo, L.; Gabler, T.; Pfanzagl, V.; Michlits, H.; Furtmueller, P.G.; Obinger, C.; Hofbauer, S.; Smulevich, G.
The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes Effect on structure and catalysis
J. Inorg. Biochem.
195
61-70
2019
Listeria monocytogenes serotype 1/2a (Q8Y5F1), Listeria monocytogenes serotype 1/2a ATCC BAA-679 (Q8Y5F1)
Lobo, S.; Scott, A.; Videira, M.; Winpenny, D.; Gardner, M.; Palmer, M.; Schroeder, S.; Lawrence, A.; Parkinson, T.; Warren, M.; Saraiva, L.
Staphylococcus aureus haem biosynthesis Characterisation of the enzymes involved in final steps of the pathway
Mol. Microbiol.
97
472-487
2015
Staphylococcus aureus (A0A0S3DY11)
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