The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site.

The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site.

Item
http://www.wikidata.org/entity/Q30580749
Crystal 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 functionDeciphering the structural role of histidine 83 for heme binding in hemophore HasAInactivation of the Heme Degrading Enzyme IsdI by an Active Site Substitution That Diminishes Heme RufflingSolution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae.Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; coupling to the distal H-bond network via ordered water molecules.Degradation of heme in gram-negative bacteria: the product of the hemO gene of Neisseriae is a heme oxygenase.Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI.How active-site protonation state influences the reactivity and ligation of the heme in chlorite dismutase.A dimeric chlorite dismutase exhibits O2-generating activity and acts as a chlorite antioxidant in Klebsiella pneumoniae MGH 78578.The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism.1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosaRoles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.
P2860

The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site.

Item
http://www.wikidata.org/entity/Q30580749
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The heme complex of Hmu O, a b ...... ructure of the catalytic site.
@ast
The heme complex of Hmu O, a b ...... ructure of the catalytic site.
@en
type
label
The heme complex of Hmu O, a b ...... ructure of the catalytic site.
@ast
The heme complex of Hmu O, a b ...... ructure of the catalytic site.
@en
prefLabel
The heme complex of Hmu O, a b ...... ructure of the catalytic site.
@ast
The heme complex of Hmu O, a b ...... ructure of the catalytic site.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P356
P1433
P1476
The heme complex of Hmu O, a b ...... tructure of the catalytic site
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698