Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis.
about
Purification and biochemical properties of phytochromobilin synthase from etiolated oat seedlingsStructure and heme binding properties ofEscherichia coliO157:H7 ChuXA review on hemeoxygenase-2: focus on cellular protection and oxygen responseIsocyanides inhibit human heme oxygenases at the verdoheme stage.Examination of the ligand-binding and enzymatic properties of a bilin-binding protein from the poisonous caterpillar Lonomia obliquaUse of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO geneIdentification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeatsThe hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.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 hemoglobin.IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Chlamydomonas reinhardtii LFO1 Is an IsdG Family Heme Oxygenase.Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism.In vivo uptake of a haem analogue Zn protoporphyrin IX by the human malaria parasite P. falciparum-infected red blood cells.Expression and biochemical properties of a ferredoxin-dependent heme oxygenase required for phytochrome chromophore synthesis.Unique features of recombinant heme oxygenase of Drosophila melanogaster compared with those of other heme oxygenases studied.Heme oxygenase-1, intermediates in verdoheme formation and the requirement for reduction equivalents.Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycle.Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae.Phytobilin biosynthesis: cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803.Structure 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.
P2860
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P2860
Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh-hant
name
Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis.
@en
type
label
Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis.
@en
prefLabel
Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis.
@en
P2093
P356
P1433
P1476
Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis.
@en
P2093
P R Ortiz de Montellano
P304
P356
10.1021/BI952405F
P407
P577
1996-01-01T00:00:00Z