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Literature summary extracted from

  • Matsui, T.; Iwasaki, M.; Sugiyama, R.; Unno, M.; Ikeda-Saito, M.
    Dioxygen activation for the self-degradation of heme: reaction mechanism and regulation of heme oxygenase (2010), Inorg. Chem., 49, 3602-3609.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.18 DTT-bound forms of ferric heme-HO-1 complexes, X-ray diffraction structure analysis of crystal structures with PDB IDSs I9T and 3I9U, resolution is 1.5 A Corynebacterium diphtheriae
1.14.14.18 thiol-bound forms of ferric heme-HO-1 complexes, thiols are from DTT or DTE, X-ray diffraction structure analysis of crystal structures with PDB IDSs I9T and 3I9U, resolution is 2.15-2.25 A Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.18 DTE binding structure, overview Corynebacterium diphtheriae
1.14.14.18 DTE shows high-affinity binding, structure, overview Homo sapiens
1.14.14.18 DTE shows high-affinity binding, structure, overview Rattus norvegicus
1.14.14.18 DTT binding structure, overview Corynebacterium diphtheriae
1.14.14.18 DTT shows high-affinity binding, structure, overview. The noncoordinating thiol group of DTT is critical for its high affinity to the mammalian HO Homo sapiens
1.14.14.18 DTT shows high-affinity binding, structure, overview. The noncoordinating thiol group of DTT is critical for its high affinity to the mammalian HO Rattus norvegicus
1.14.14.18 additional information development of HO-specific inhibitors targeting the critical distal hydrogen bonding network, e.g. thiol compounds, overview. HmuO exhibits similar affinity for DTT, DTE, and thioglycerol in contrast to the mammalian enzyme, indicating no functionality of the noncoordinating thiol group in complex formation with this bacterial HO Corynebacterium diphtheriae
1.14.14.18 additional information development of HO-specific inhibitors targeting the critical distal hydrogen bonding network, e.g. thiol compounds, overview. Thiol binding significantly suppresses but does not completely interrupt the reduction of the ferric heme to the ferrous state. HO is inhibited thus at higher thiol concentration than expected from the dissociation equilibrium constants Homo sapiens
1.14.14.18 additional information development of HO-specific inhibitors targeting the critical distal hydrogen bonding network, e.g. thiol compounds, overview. Thiol binding significantly suppresses but does not completely interrupt the reduction of the ferric heme to the ferrous state. HO is inhibited thus at higher thiol concentration than expected from the dissociation equilibrium constants Rattus norvegicus
1.14.14.18 thioglycerol binds weakly, shows high affinity to the mammalian HO Corynebacterium diphtheriae
1.14.14.18 thioglycerol binds with 10fold lower affinity than DTT, shows high affinity to the mammalian HO Homo sapiens
1.14.14.18 thioglycerol binds with 10fold lower affinity than DTT, shows high affinity to the mammalian HO Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.18 heme + 3 AH2 + 3 O2 Homo sapiens requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2 Corynebacterium diphtheriae requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2 Rattus norvegicus requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 additional information Homo sapiens The first HO reaction step is the regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, the second is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. The third reaction step is a major rate-determining step of HO catalysis to regulate the enzyme activity. HO catalysis is unique in that all three O2 activations are performed by the substrate itself, analysis of structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps, overview. FeOOH verdoheme is the key intermediate of the ring-opening reaction, mechanism, overview. Critical functioning of the FeOOH species in HO heme self-oxidation and catalytic importance of the distal hydrogen bonding network in its unique O2 activation ?
-
 ?
1.14.14.18 additional information Corynebacterium diphtheriae The first HO reaction step is the regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, the second is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. The third reaction step is a major rate-determining step of HO catalysis to regulate the enzyme activity. HO catalysis is unique in that all three O2 activations are performed by the substrate itself, analysis of structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps, overview. FeOOH verdoheme is the key intermediate of the ring-opening reaction, mechanism, overview. Critical functioning of the FeOOH species in HO heme self-oxidation and catalytic importance of the distal hydrogenbonding network in its unique O2 activation ?
-
 ?
1.14.14.18 additional information Rattus norvegicus The first HO reaction step is the regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, the second is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. The third reaction step is a major rate-determining step of HO catalysis to regulate the enzyme activity. HO catalysis is unique in that all three O2 activations are performed by the substrate itself, analysis of structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps, overview. FeOOH verdoheme is the key intermediate of the ring-opening reaction, mecjanism, overview. Critical functioning of the FeOOH species in HO heme self-oxidation and catalytic importance of the distal hydrogenbonding network in its unique O2 activation ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.18 Corynebacterium diphtheriae
-
-
-
1.14.14.18 Homo sapiens
-
 two isoforms, an inducible HO-1 and a constitutive HO-2
-
1.14.14.18 Rattus norvegicus P06762 two isoforms, an inducible HO-1 and a constitutive HO-2
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.18 heme + 3 AH2 + 3 O2 requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview Homo sapiens biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2 requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview Corynebacterium diphtheriae biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 heme + 3 AH2 + 3 O2 requires three oxidative reaction steps, via alpha-meso-hydroxy-heme and verdoheme, detailed overview Rattus norvegicus biliverdin + Fe2+ + CO + 3 A + 3 H2O
-
 ?
1.14.14.18 additional information The first HO reaction step is the regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, the second is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. The third reaction step is a major rate-determining step of HO catalysis to regulate the enzyme activity. HO catalysis is unique in that all three O2 activations are performed by the substrate itself, analysis of structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps, overview. FeOOH verdoheme is the key intermediate of the ring-opening reaction, mechanism, overview. Critical functioning of the FeOOH species in HO heme self-oxidation and catalytic importance of the distal hydrogen bonding network in its unique O2 activation Homo sapiens ?
-
 ?
1.14.14.18 additional information The first HO reaction step is the regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, the second is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. The third reaction step is a major rate-determining step of HO catalysis to regulate the enzyme activity. HO catalysis is unique in that all three O2 activations are performed by the substrate itself, analysis of structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps, overview. FeOOH verdoheme is the key intermediate of the ring-opening reaction, mechanism, overview. Critical functioning of the FeOOH species in HO heme self-oxidation and catalytic importance of the distal hydrogenbonding network in its unique O2 activation Corynebacterium diphtheriae ?
-
 ?
1.14.14.18 additional information The first HO reaction step is the regiospecific hydroxylation of the porphyrin alpha-meso-carbon atom, the second is a rapid, spontaneous autooxidation of the reactive alpha-meso-hydroxyheme in which the HO enzyme does not play a critical role. The third reaction step is a major rate-determining step of HO catalysis to regulate the enzyme activity. HO catalysis is unique in that all three O2 activations are performed by the substrate itself, analysis of structural and biochemical properties of HO catalysis, especially its first and third oxygenation steps, overview. FeOOH verdoheme is the key intermediate of the ring-opening reaction, mecjanism, overview. Critical functioning of the FeOOH species in HO heme self-oxidation and catalytic importance of the distal hydrogenbonding network in its unique O2 activation Rattus norvegicus ?
-
 ?
1.14.14.18 additional information structure-function relationship and analysis, overview Homo sapiens ?
-
 ?
1.14.14.18 additional information structure-function relationship and analysis, overview Corynebacterium diphtheriae ?
-
 ?
1.14.14.18 additional information structure-function relationship and analysis, overview Rattus norvegicus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.14.18 HmuO
-
 Corynebacterium diphtheriae
1.14.14.18 HO-1
-
 Homo sapiens
1.14.14.18 HO-1
-
 Rattus norvegicus
1.14.14.18 HO-2
-
 Homo sapiens

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.14.14.18 0.017
-
 isozyme HO-1, pH not specified in the publication, temperature not specified in the publication Homo sapiens DTE
1.14.14.18 1.2
-
 isozyme HO-2, pH not specified in the publication, temperature not specified in the publication Homo sapiens DTE

General Information

EC Number General Information Comment Organism
1.14.14.18 additional information modulation of HO catalysis by ligands targeting the critical distal pocket structure, overview Homo sapiens
1.14.14.18 additional information modulation of HO catalysis by ligands targeting the critical distal pocket structure, overview Corynebacterium diphtheriae
1.14.14.18 additional information modulation of HO catalysis by ligands targeting the critical distal pocket structure, overview Rattus norvegicus