Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae

scientific article published in July 1999

Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.274.30.21319
P698PubMed publication ID10409691
P5875ResearchGate publication ID12889143

P2093author name stringX Zhang
T Yoshida
K Katakura
M Ikeda-Saito
G C Chu
P2860cites workHeme oxygenase 2: endothelial and neuronal localization and role in endothelium-dependent relaxationQ33580047
Heme-Containing OxygenasesQ34114428
Carbon Monoxide: a Putative Neural MessengerQ34305648
Genetics and regulation of heme iron transport in Shigella dysenteriae and detection of an analogous system in Escherichia coli O157:H7.Q35586588
Cloning, sequence, and footprint analysis of two promoter/operators from Corynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and ironQ36105374
Heme oxygenase 1 is required for mammalian iron reutilizationQ36601831
Iron, DtxR, and the regulation of diphtheria toxin expressionQ36713387
Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobinQ36843552
Quelling the red menace: haem capture by bacteriaQ41070988
Transport of haemin across the cytoplasmic membrane through a haemin-specific periplasmic binding-protein-dependent transport system in Yersinia enterocoliticaQ41498750
Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysisQ46078167
Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycleQ46466951
Histidine-132 does not stabilize a distal water ligand and is not an important residue for the enzyme activity in heme oxygenase-1.Q54567522
Heme Oxygenase-2Q56837992
The Molar Light Absorption of Pyridine Ferroprotoporphrin (Pyridine Haemochromogen)Q100807771
P433issue30
P407language of work or nameEnglishQ1860
P921main subjectCorynebacterium diphtheriaeQ131649
P304page(s)21319-21325
P577publication date1999-07-01
P1433published inJournal of Biological ChemistryQ867727
P1476titleHeme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae
P478volume274

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cites work (P2860)
Q92816996Artificial Hydrogenases Based on Cobaloximes and Heme Oxygenase
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Q54454286Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193.
Q36076532Structure prediction and activity analysis of human heme oxygenase-1 and its mutant
Q37348889Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation
Q27642658The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae
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Q95434328Tyrosine oxidation in heme oxygenase: examination of long-range proton-coupled electron transfer
Q33993547Use of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO gene

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