Pages that link to "Q27641460"
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The following pages link to Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation (Q27641460):
Displaying 26 items.
- Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase (Q24310223) (← links)
- The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae (Q27642658) (← links)
- Ruffling of Metalloporphyrins Bound to IsdG and IsdI, Two Heme-degrading Enzymes in Staphylococcus aureus (Q27651684) (← links)
- The IsdG-family of haem oxygenases degrades haem to a novel chromophore (Q27660036) (← links)
- Crystal structure of the Pseudomonas aeruginosa cytoplasmic heme binding protein, Apo-PhuS (Q27679794) (← links)
- 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 (Q31039839) (← links)
- 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 (Q33237045) (← links)
- 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 (Q33243618) (← links)
- Diatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa (Q33263176) (← links)
- Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase (Q33511502) (← links)
- Identification and characterization of AckA-dependent protein acetylation in Neisseria gonorrhoeae (Q33842204) (← links)
- Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI. (Q33970868) (← links)
- Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes (Q34433464) (← links)
- 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 (Q35648424) (← links)
- Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance study (Q36445749) (← links)
- 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 (Q37178924) (← links)
- 1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure (Q37298678) (← links)
- Signaling function of heme oxygenase proteins. (Q37653688) (← links)
- Hyperoxia attenuates the inhibitory effect of nitric oxide donors on HIF prolyl-4-hydroxylase-2: Implication on discriminative effect of nitric oxide on HIF prolyl-4-hydroxylase-2 and collagen prolyl-4-hydroxylase. (Q37715426) (← links)
- Novel lead structures and activation mechanisms for CO-releasing molecules (CORMs) (Q38195891) (← links)
- Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism. (Q41237558) (← links)
- Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism. (Q45140492) (← links)
- Crystal structures of the G139A, G139A-NO and G143H mutants of human heme oxygenase-1. A finely tuned hydrogen-bonding network controls oxygenase versus peroxidase activity (Q46428883) (← links)
- Structure-based design and biological evaluation of inhibitors of the pseudomonas aeruginosa heme oxygenase (pa-HemO). (Q49833934) (← links)
- Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193. (Q54454286) (← links)
- FeGenie: A Comprehensive Tool for the Identification of Iron Genes and Iron Gene Neighborhoods in Genome and Metagenome Assemblies (Q89820544) (← links)