scholarly article | Q13442814 |
P50 | author | Gerd La Mar | Q106870083 |
P2093 | author name string | Tadashi Yoshida | |
Yangzhong Liu | |||
Xuhong Zhang | |||
James D Satterlee | |||
Li-Hua Ma | |||
P2860 | cites work | Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1 | Q27634857 |
Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide. Implication for regiospecific hydroxylation of heme at the alpha-meso carbon | Q27639657 | ||
Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation | Q27641460 | ||
Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications | Q27641631 | ||
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The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae | Q27642658 | ||
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The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase | Q28181839 | ||
Hydrogen exchange and structural dynamics of proteins and nucleic acids | Q28262950 | ||
Mechanism of heme degradation by heme oxygenase | Q29397702 | ||
Solution NMR characterization of an unusual distal H-bond network in the active site of the cyanide-inhibited, human heme oxygenase complex of the symmetric substrate, 2,4-dimethyldeuterohemin | Q30698820 | ||
1H NMR detection of immobilized water molecules within a strong distal hydrogen-bonding network of substrate-bound human heme oxygenase-1. | Q30749480 | ||
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 | Q30754996 | ||
Solution 1H, 15N NMR Spectroscopic Characterization of Substrate-Bound, Cyanide-Inhibited Human Heme Oxygenase: Water Occupation of the Distal Cavity | Q30882990 | ||
1H NMR investigation of the solution structure of substrate-free human heme oxygenase: comparison to the cyanide-inhibited, substrate-bound complex | Q30885667 | ||
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Solution 1H NMR characterization of the distal H-bond network and the effective axial field in the resting-state, high-spin ferric, substrate-bound complex of heme oxygenase from N. meningitidis | Q33214416 | ||
Degradation of heme in gram-negative bacteria: the product of the hemO gene of Neisseriae is a heme oxygenase | Q33792508 | ||
The mechanism of heme oxygenase | Q33878368 | ||
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Real-time solvent exchange studies of the imino and amino protons of yeast phenylalanine transfer RNA by Fourier transform NMR | Q37335432 | ||
Importance of histidine residue 25 of rat heme oxygenase for its catalytic activity | Q38330515 | ||
Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa | Q39529862 | ||
Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system | Q39600963 | ||
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Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme | Q42641232 | ||
Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme. | Q44244382 | ||
Stereoselectivity of each of the three steps of the heme oxygenase reaction: hemin to meso-hydroxyhemin, meso-hydroxyhemin to verdoheme, and verdoheme to biliverdin | Q44479675 | ||
Essential Amino Acid Residues Controlling the Unique Regioselectivity of Heme Oxygenase in Pseudomonas aeruginosa | Q44834522 | ||
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Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxylating species | Q46114677 | ||
Structural basis for novel delta-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa | Q46184086 | ||
Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycle | Q46466951 | ||
Disruption of an active site hydrogen bond converts human heme oxygenase-1 into a peroxidase | Q95717606 | ||
P433 | issue | 12 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Neisseria meningitidis | Q154625 |
P304 | page(s) | 3875-3886 | |
P577 | publication date | 2006-03-01 | |
P1433 | published in | Biochemistry | Q764876 |
P1476 | title | 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 | |
P478 | volume | 45 |
Q37298678 | 1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure |
Q24296465 | Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase |
Q35648424 | Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study |
Q36445749 | Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance study |
Q34433464 | Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes |