Heme degradation by Staphylococcus aureus IsdG and IsdI liberates formaldehyde rather than carbon monoxide.
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Formaldehyde Stress Responses in Bacterial PathogensCrystallographic and Spectroscopic Insights into Heme Degradation by Mycobacterium tuberculosis MhuDIn vitro heme biotransformation by the HupZ enzyme from Group A streptococcusSubstrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and hemeHeme uptake in bacterial pathogensMetal limitation and toxicity at the interface between host and pathogenThe PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Dynamic ruffling distortion of the heme substrate in non-canonical heme oxygenase enzymes.Time-resolved Studies of IsdG Protein Identify Molecular Signposts along the Non-canonical Heme Oxygenase PathwayUnique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation.The Effectors and Sensory Sites of Formaldehyde-responsive Regulator FrmR and Metal-sensing VariantSequestration and scavenging of iron in infection.Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation.Radical new paradigm for heme degradation in Escherichia coli O157:H7.A selective stepwise heme oxygenase model system: an iron(IV)-oxo porphyrin π-cation radical leads to a verdoheme-type compound via an isoporphyrin intermediate.Reactions of Ferrous Coproheme Decarboxylase (HemQ) with O2 and H2O2 Yield Ferric Heme b.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Chlamydomonas reinhardtii LFO1 Is an IsdG Family Heme Oxygenase.Reaction intermediates in the heme degradation reaction by HutZ from Vibrio cholerae.Tight binding of heme to Staphylococcus aureus IsdG and IsdI precludes design of a competitive inhibitor.Hydrogen bond donation to the heme distal ligand of Staphylococcus aureus IsdG tunes the electronic structure.Involvement of reductases IruO and NtrA in iron acquisition by Staphylococcus aureus.Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin.The influence of heme ruffling on spin densities in ferricytochromes c probed by heme core 13C NMR.IruO is a reductase for heme degradation by IsdI and IsdG proteins in Staphylococcus aureus.Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes.Density functional study of porphyrin distortion effects on redox potential of heme.Energetics underlying hemin extraction from human hemoglobin by Staphylococcus aureus.From Host Heme To Iron: The Expanding Spectrum of Heme Degrading Enzymes Used by Pathogenic Bacteria.
P2860
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P2860
Heme degradation by Staphylococcus aureus IsdG and IsdI liberates formaldehyde rather than carbon monoxide.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Heme degradation by Staphyloco ...... e rather than carbon monoxide.
@en
type
label
Heme degradation by Staphyloco ...... e rather than carbon monoxide.
@en
prefLabel
Heme degradation by Staphyloco ...... e rather than carbon monoxide.
@en
P2093
P2860
P356
P1433
P1476
Heme degradation by Staphyloco ...... de rather than carbon monoxide
@en
P2093
Celia W Goulding
Kouhei Tsumoto
Masao Ikeda-Saito
Shusuke Nambu
Yukari Ono
P2860
P304
P356
10.1021/BI400382P
P407
P577
2013-04-24T00:00:00Z