Degradation of heme in gram-negative bacteria: the product of the hemO gene of Neisseriae is a heme oxygenase.
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Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humansRole of Nrf2/HO-1 system in development, oxidative stress response and diseases: an evolutionarily conserved mechanismCrystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activationThe crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriaeCrystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase functionUnusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosisThe IsdG-family of haem oxygenases degrades haem to a novel chromophoreIn vitro heme biotransformation by the HupZ enzyme from Group A streptococcusRv2074 is a novel F420 H2 -dependent biliverdin reductase in Mycobacterium tuberculosisRegulation of intracellular heme levels by HMX1, a homologue of heme oxygenase, in Saccharomyces cerevisiae.Heme degrading protein HemS is involved in oxidative stress response of Bartonella henselaeBacillus subtilis Fur represses one of two paralogous haem-degrading monooxygenases.Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases.Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae.1H NMR investigation of the solution structure of substrate-free human heme oxygenase: comparison to the cyanide-inhibited, substrate-bound complex.Characterization of heme uptake cluster genes in the fish pathogen Vibrio anguillarum.Characterization of the spontaneous "aging" of the heme oxygenase from the pathological bacterium Neisseria meningitidis via cleavage of the C-terminus in contact with the substrate. Implications for functional studies and the crystal structure.1H NMR study of the magnetic properties and electronic structure of the hydroxide complex of substrate-bound heme oxygenase from Neisseria meningitidis: influence of the axial water deprotonation on the distal H-bond network.Diatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa.Host iron binding proteins acting as niche indicators for Neisseria meningitidisIdentification and characterization of AckA-dependent protein acetylation in Neisseria gonorrhoeae.Identification of the iron-responsive genes of Neisseria gonorrhoeae by microarray analysis in defined medium.Transition metals at the host-pathogen interface: how Neisseria exploit human metalloproteins for acquiring iron and zinc.Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicityAntimicrobial properties of porphyrins.Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeatsCandida albicans heme oxygenase and its product CO contribute to pathogenesis of candidemia and alter systemic chemokine and cytokine expressionBacillus anthracis IsdG, a heme-degrading monooxygenaseOvercoming the heme paradox: heme toxicity and tolerance in bacterial pathogens.The effect of iron limitation on the transcriptome and proteome of Pseudomonas fluorescens Pf-5.Heme enzyme structure and function.Crystal structure of HutZ, a heme storage protein from Vibrio cholerae: A structural mismatch observed in the region of high sequence conservation.HutZ is required for efficient heme utilization in Vibrio choleraeThe crimson conundrum: heme toxicity and tolerance in GAS.Characterization of five ECF sigma factors in the genome of Pseudomonas syringae pv. syringae B728aMicrobial iron acquisition: marine and terrestrial siderophores.The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.Heme utilization in Campylobacter jejuni.Pyrophosphate-mediated iron acquisition from transferrin in Neisseria meningitidis does not require TonB activity.Iron transport systems in Neisseria meningitidis
P2860
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P2860
Degradation of heme in gram-negative bacteria: the product of the hemO gene of Neisseriae is a heme oxygenase.
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Degradation of heme in gram-ne ...... eisseriae is a heme oxygenase.
@ast
Degradation of heme in gram-ne ...... eisseriae is a heme oxygenase.
@en
type
label
Degradation of heme in gram-ne ...... eisseriae is a heme oxygenase.
@ast
Degradation of heme in gram-ne ...... eisseriae is a heme oxygenase.
@en
prefLabel
Degradation of heme in gram-ne ...... eisseriae is a heme oxygenase.
@ast
Degradation of heme in gram-ne ...... eisseriae is a heme oxygenase.
@en
P2093
P2860
P1476
Degradation of heme in gram-ne ...... eisseriae is a heme oxygenase.
@en
P2093
P2860
P304
P356
10.1128/JB.182.23.6783-6790.2000
P407
P577
2000-12-01T00:00:00Z