scholarly article | Q13442814 |
P356 | DOI | 10.1074/JBC.M410263200 |
P8608 | Fatcat ID | release_h35b4b5ej5evtpzihsmvqofe3i |
P698 | PubMed publication ID | 15528205 |
P50 | author | Toshitaka Matsui | Q51115171 |
Takeshi Tomita | Q57446183 | ||
P2093 | author name string | Masaki Unno | |
Masao Ikeda-Saito | |||
Momoko Furukawa | |||
P2860 | cites work | Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycle | Q46466951 |
Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae | Q47946397 | ||
Porphyrin traps its terminator! Concerted and stepwise porphyrin degradation mechanisms induced by heme-oxygenase and cytochrome p450. | Q51019851 | ||
Human heme oxygenase cDNA and induction of its mRNA by hemin | Q24298146 | ||
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination | Q26778405 | ||
Processing of X-ray diffraction data collected in oscillation mode | Q26778468 | ||
Crystal structure of rat heme oxygenase-1 in complex with heme | Q27622187 | ||
Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1 | Q27634857 | ||
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 | ||
Crystal structures of ferrous and CO-, CN(-)-, and NO-bound forms of rat heme oxygenase-1 (HO-1) in complex with heme: structural implications for discrimination between CO and O2 in HO-1 | Q27641850 | ||
Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function | Q27643141 | ||
The CCP4 suite: programs for protein crystallography | Q27861090 | ||
The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site. | Q30580749 | ||
Emerging strategies in microbial haem capture. | Q30636480 | ||
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 | ||
Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores | Q33879806 | ||
Use of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO gene | Q33993547 | ||
Reduced stress defense in heme oxygenase 1-deficient cells. | Q36601994 | ||
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 | Q36843552 | ||
The Arabidopsis thaliana HY1 locus, required for phytochrome-chromophore biosynthesis, encodes a protein related to heme oxygenases | Q37215294 | ||
Resonance Raman studies of nitric oxide binding to ferric and ferrous hemoproteins: detection of Fe(III)--NO stretching, Fe(III)--N--O bending, and Fe(II)--N--O bending vibrations | Q37512641 | ||
The heme oxygenase system: a regulator of second messenger gases | Q41455806 | ||
Crystal structure of human heme oxygenase-1. | Q41687640 | ||
Replacement of the distal glycine 139 transforms human heme oxygenase-1 into a peroxidase | Q41755561 | ||
A role for highly conserved carboxylate, aspartate-140, in oxygen activation and heme degradation by heme oxygenase-1. | Q43663150 | ||
Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme. | Q44244382 | ||
Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants | Q45712309 | ||
Structural basis for novel delta-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa | Q46184086 | ||
P433 | issue | 4 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Corynebacterium diphtheriae | Q131649 |
P1104 | number of pages | 9 | |
P304 | page(s) | 2981-2989 | |
P577 | publication date | 2004-11-04 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism | |
P478 | volume | 280 |
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Q34433464 | Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes |
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Q27660036 | The IsdG-family of haem oxygenases degrades haem to a novel chromophore |
Q37178924 | 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 |
Q95434328 | Tyrosine oxidation in heme oxygenase: examination of long-range proton-coupled electron transfer |
Q36802518 | Unique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation |
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