1.14.14.18 15-phenylheme + electron donor + O2 - Homo sapiens 10-phenylbiliverdin IXalpha + Fe2+ + CO + oxidized eletron donor + H2O - ? 375578 1.14.14.18 5-phenylheme + electron donor + O2 - Homo sapiens biliverdin IXalpha + Fe2+ + CO + oxidized eletron donor + H2O + benzoic acid - ? 376008 1.14.14.18 alpha-meso-formylmesoheme + NADPH exclusively oxidized at a non-formyl substituted meso-carbon Homo sapiens ? + NADP+ - ? 287921 1.14.14.18 alpha-meso-hydroxyhemin IX + reduced acceptor + O2 - Rattus norvegicus verdoheme IXalpha + CO + acceptor + H2O - ? 376244 1.14.14.18 alpha-meso-oxyprotoheme IX + [reduced NADPH-hemoprotein reductase] + O2 - Bos taurus ? - r 451306 1.14.14.18 beta-meso-hydroxyhemin IX + reduced acceptor + O2 - Rattus norvegicus verdoheme IXbeta + CO + acceptor + H2O - ? 376405 1.14.14.18 Co-heme + NADPH + H+ + O2 - Rattus norvegicus biliverdin Ixalpha + Co2+ + CO + NAD+ + H2O - r 451307 1.14.14.18 delta-meso-hydroxyhemin IX + reduced acceptor + O2 - Rattus norvegicus verdoheme IXdelta + CO + acceptor + H2O - ? 376664 1.14.14.18 Fe-heme + [reduced NADPH-hemoprotein reductase] + O2 - Rattus norvegicus biliverdin Ixalpha + Fe2+ + CO + NAD+ + H2O - r 451308 1.14.14.18 gamma-CH-Fe(cor) + 3 AH2 + 3 O2 the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview Arabidopsis thaliana ? - ? 417021 1.14.14.18 gamma-CH-Fe(cor) + 3 AH2 + 3 O2 the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview Synechocystis sp. ? - ? 417021 1.14.14.18 gamma-meso-hydroxyhemin IX + reduced acceptor + O2 - Rattus norvegicus verdoheme IXgamma + CO + acceptor + H2O - ? 376817 1.14.14.18 hematoheme + NADPH + H+ + O2 - Rattus norvegicus hematobiliverdin Fe2+ + CO + NAD+ + H2O - r 451310 1.14.14.18 heme + 2 NADH + 2 H+ + 2 O2 NADH-dependent heme degradation system may have a biological role in regulating the concentration of respiratory hemoproteins and the disposition of the aberrant forms of the mitochondrial hemoproteins Bos taurus biliverdin + Fe2+ + CO + 2 NAD+ + H2O - ? 370239 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 - Gallus gallus biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 - Homo sapiens biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 - Rattus norvegicus biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 - Bos taurus biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 involved in heme metabolism Gallus gallus biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 involved in heme metabolism Homo sapiens biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 involved in heme metabolism Rattus norvegicus biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 involved in heme metabolism Sus scrofa biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 involved in heme metabolism Bos taurus biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 2 NADPH + 2 H+ + 2 O2 involved in heme metabolism Oryctolagus cuniculus biliverdin + Fe2+ + CO + 2 NADP+ + H2O - ? 370238 1.14.14.18 heme + 3 AH2 + 3 O2 - Homo sapiens biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 - Neisseria meningitidis biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 - Campylobacter jejuni biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 - Rattus norvegicus biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 - Corynebacterium diphtheriae biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 - Medicago sativa biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 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 - ? 415652 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 - ? 415652 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 - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2 Homo sapiens biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2 Rattus norvegicus biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 reaction intermediate verdoheme and the verdoheme-enzyme complex are gradually degraded in the presence of O2 Corynebacterium diphtheriae biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 - Rattus norvegicus Sprague-Dawley biliverdin + Fe2+ + CO + 3 A + 3 H2O - ? 415652 1.14.14.18 heme + 3 AH2 + 3 O2 - Helicobacter pylori biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O - ? 415653 1.14.14.18 heme + 3 AH2 + 3 O2 - Brassica rapa subsp. pekinensis biliverdin IXalpha + Fe2+ + CO + 3 A + 3 H2O - ? 415653 1.14.14.18 heme + 3 reduced ascorbate + 3 O2 - Neisseria meningitidis biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O - ? 428677 1.14.14.18 heme + 3 reduced ascorbate + 3 O2 - Campylobacter jejuni biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O - ? 428677 1.14.14.18 heme + AH2 + O2 - Cricetulus griseus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 - Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 - Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 - Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 - Neisseria meningitidis biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 - Bos taurus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 activation of the enzyme leads to induction of the ABC transporter ABCG2, but not of ABCB6 Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 biliverdin is involved in hemin degradation Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 CO plays a role in cGMP production, p38 mitogen-activated protein kinase activation, and nuclear factor-kB activation, as part of the heme oxygenase-1/carbon monoxide, HO-1/CO, system, overview, correlation of HO-1-mediated cytoprotection with a decrease in intracellular free iron amounts. Biliverdin is a third generated heme catabolite by HO-1 and is converted to bilirubin by the catalytic reaction of biliverdin reductase. Both compounds are reducing species and hence may play a role in the protective response to vascular injury by oxidative stress Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 endogenous HO-1 shows anti-apoptotic activity, and is overexpressed in various cancer diseases and might contribute to cancer progression Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 exogenous CO activates Nrf2 through the phosphorylation of protein kinase R-like endoplasmic reticulum kinase, resulting in HO-1 expression, mechanism, overview, CO renders endothelial cells resistant to ER stress not only by downregulating C/EBP homologous protein expression via p38 mitogen-activated protein kinase activation but also by upregulating Nrf2-dependent HO-1 expression via PERK activation Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 first step in the heme degradation pathway Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 heat shock factor 1, HSF1, is directly involved in the transcriptional regulation of ho-1 mediated by the enzyme's cadmium-responsive element, mechanism, overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 heme degradation Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 heme oxygenase is the rate-limiting enzyme in heme degradation to biliverdin, heme oxygenase-1 catalyzes the degradation of heme and forms antioxidant bile pigments as well as the signaling molecule carbon monoxide, HO-1 is inducible in response to a variety of chemical and physical stress conditions to function as a cytoprotective molecule. Catalytic inactive heme oxygenase-1 deletion mutant protein regulates its own expression in oxidative stress in a positive feedback manner, feed-forward autoregulation of HO-1 in oxidative stress, overview, HO-1 protein also plays a role in regulating cadmium chloride-mediated HO-1 gene induction Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 heme oxygenase-1 is regulated by the Nrf2/anti-oxidant response element, ARE, pathway, which plays an important role in regulating cellular anti-oxidants Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 heme oxygenase-1 upregulation significantly inhibits TNF-alpha and Hmgb1 releasing and attenuates lipopolysaccharide-induced acute lung injury in mice, overview Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO is a microsomal enzyme and catalyzes the oxidation of the alpha-meso-carbon bridge of heme moieties resulting in the generation of ferrous iron, carbon monoxide and biliverdin. HO-1 is inducible and plays a main role in the cellular oxidant/antioxidant balance, whereas HO-2 is constitutive and involved in the physiologicalmetabolism of heme Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 acts as anti-oxidant and protects cells against injury, it regulates neutrophil O2- production and protects the intestine from damage following EtOH and burn injury, overview Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 catalyzes the rate-limiting step of heme degradation and plays an important anti-inflammatory role via its enzymatic products carbon monoxide and biliverdin Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 catalyzes the rate-limiting step of heme degradation and plays an important anti-inflammatory role via its enzymatic products carbon monoxide and biliverdin Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 exhibits cytoprotective function, enzyme induction, e.g. by dehydrocostus lactone, causes the nuclear accumulation of the nuclear factor E2-related factor 2, Nrf2, and increases the promoter activity of antioxidant response element, ARE, overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 gene is a glia-expressing wound-responsive gene, HO-1 gene expression associated with traumatic brain injury involving the toll-like receptor 2, overview Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 induction in vivo inhibits cytokine production in synovial tissue, while HO-1 inhibition restores it, overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 is a cell-protective anti-oxidant enzyme, which is sensitively induced by oxidative stress and regulated by oxidized-1-palmitoyl-2-arachidonoyl-sn-glycerol-3-phosphocholine, i.e. Ox-PAPC, and Nrf2, overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 is a critical cell defence enzyme against oxidative stress, HO-1 participates in the protective effect afforded by neuronal nicotinic acetylcholine receptors, nAChR, activation, which activates the neuroprotective signaling cascade, overview Bos taurus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 is a heat shock protein, and it provides endogenous anti-oxidant and anti-inflammatory moieties which can modulate colonic inflammation Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 is a key enzyme in the cellular response to tissue injury and oxidative stress. HO-1 enzymatic activity results in the formation of the cytoprotective metabolites CO and biliverdin Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 is an antioxidant and cytoprotective enzyme. Methoxychalcones, especially 5-methoxychalcone, 3,4,5-trimethoxychalcone, and 3,4,5,3',4',5'-hexamethoxychalcone, induce the enzyme expression and activity in macrophages without causing cytotoxicity, they also cause anti-inflamatory affects, overview Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 is an inducible enzyme that catalyzes the rate-limiting step in the degradation of heme to biliverdin, CO and iron Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin. HO-1 receives the electrons necessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase, CPR, releasing free iron and carbon monoxide Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 is the rate-limiting enzyme in heme degradation Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 is the rate-limiting enzyme in heme degradation Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 participates in the degradation of heme, the enzyme is involved in tumor development Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 participates in the degradation of heme, the enzyme is involved in tumor development Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 shows anti-inflammatory effect, inhibition of HO-1 or scavenging of CO significantly reverses the inhibition of LPS-stimulated nitrite accumulation by tanshinone IIA, overview Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 shows anti-inflammatory properties Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 shows vasculoprotective and anti-inflammatory activity, it is ptionally regulated by peroxisome proliferator-activated receptors PPARalpha and PPARgamma in vascular cells, inhibition of HO-1 enzymatic activity reverses PPAR ligand-mediated inhibition of cell proliferation and expression of cyclooxygenase-2 in vascular smooth muscle cells, overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 transcriptional regulation system, overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 in aortic smooth muscle cells, induction of HO-1 confers vascular protection against cellular proliferation mainly via its up-regulation of the cyclin-dependent kinase inhibitor p21WAF1/CIP1 that is involved in negative regulation of cellular proliferation, overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 in vascular smooth muscle cells, induction of HO-1 confers vascular protection against cellular proliferation mainly via its up-regulation of the cyclin-dependent kinase inhibitor p21WAF1/CIP1 that is involved in negative regulation of cellular proliferation, overview Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 induction of HO-1 leads to a reduction of superoxide and increases levels of spermine-NoNoate, HO-1 is involved in artery vascular relaxation, overview Bos taurus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 induction of HO-1 via the ERK-Nrf2-ARE signaling pathway is involved in protecting cells from oxidative stress, overview Cricetulus griseus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 inhibition or selective knockdown of HO-1 has anti-inflammatory effects via bilirubin, overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 statin-induced heme oxygenase-1 increases NF-kappaB activation and oxygen radical production in cultured neuronal cells exposed to lipopolysaccharide, overview Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 statin-induced heme oxygenase-1 increases NF-kappaB activation and oxygen radical production in cultured neuronal cells exposed to lipopolysaccharide, overview Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 the enzyme catalyzes the first and rate-limiting step in the oxidative heme breakdown, physiological role of isozyme HO-1 and its reaction products, detailed overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 the enzyme catalyzes the first and rate-limiting step in the oxidative heme breakdown, physiological role of isozyme HO-1 and its reaction products, detailed overview Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 the enzyme catalyzes the first and rate-limiting step in the oxidative heme breakdown, physiological role of isozyme HO-2 and its reaction products, detailed overview Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 the enzyme catalyzes the first and rate-limiting step in the oxidative heme breakdown, physiological role of isozyme HO-2 and its reaction products, detailed overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 the enzyme has anti-inflammatory activity and is involved in mediation of curcumin's inhibitory effect on inducible NO synthase expression and NO production. Treatment with HO inhibitor abolishes the inhibitory effect of curcumin on lipopolysaccharide-induced NF-kappaB activation, overview Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 the enzyme plays a protective role against hypoxic injury, and in the vicious cycle of low-flow priapism Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 the enzyme shows anti-inflammatory activity, HO-1 expression is induced via the ERK1/2 activation pathway Mus musculus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 the gene encoding HO-1 is a Nrf2-regulated gene. NF-E2 related factor 2 activation and heme oxygenase-1 induction by tert-butylhydroquinone protect against deltamethrin-mediated oxidative stress in PC12 cells, e.g. by H2O2 and 6-hydroxydopamine Rattus norvegicus biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His45, resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr154, Lys199, and Arg203 orient the heme through direct interactions with the heme propionates, overview Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 the C-terminal 23 amino acids are essential for maximal catalytic activity Homo sapiens biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 - Mus musculus C57BL/6 biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 shows anti-inflammatory properties Mus musculus C57BL/6 biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 HO-1 gene is a glia-expressing wound-responsive gene, HO-1 gene expression associated with traumatic brain injury involving the toll-like receptor 2, overview Mus musculus C57BL/6 biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 - Mus musculus C3H/HEN biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + AH2 + O2 endogenous HO-1 shows anti-apoptotic activity, and is overexpressed in various cancer diseases and might contribute to cancer progression Mus musculus C3H/HEN biliverdin + Fe2+ + CO + A + H2O - ? 394867 1.14.14.18 heme + electron donor + O2 - Mus musculus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 - Homo sapiens biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 - Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 - Glycine max biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 - Neisseria meningitidis biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 - Clostridium tetani biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 NADH can replace NADPH at concentrations higher than 5 mM in vitro, NADH is unlikely to be an electron donor in vivo Bos taurus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 overview, substrate specificity Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 electron donor NADH Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 electron donor NADH Bos taurus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin Gallus gallus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin Homo sapiens biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin Sus scrofa biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin Bos taurus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 iron-protoporphyrin IX is the most active substrate, lower activity with: iron-mesoporphyrin IX, iron-deuteroheme IX, iron-coproheme I, alpha and beta chain of hemoglobin, poor substrates: oxyhemoglobin, carboxyhemoglobin, myoglobin Oryctolagus cuniculus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 alpha-meso-oxyprotoheme is an intermediate of heme degradation that is converted stereospecifically into biliverdin IXa via verdoheme IXa Bos taurus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 Ni, Mn, and Sn protoporphyrin IX is not oxidized Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 oxidation of Co-heme Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 synthetic hemins XIII and III and iron porphyrin are better substrates than the natural substrate hemin IX, 83 and 86% of hemin IX activity with mesohemin IX and hematohemin IX respectively Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 enzyme oxidizes protoheme, hematoheme, hematoheme dimethyl ester, dicysteinyl hematoheme, and heme undecapeptide, conversion of hematoheme to hematobilirubin requires the presence of: NADPH, NADPH-cytochrome c reductase, biliverdin reductase and O2 Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 testis heme oxygenase 2 oxidizes Fe-protopophyrin, ferric hematoporphyrin acetate and ferric hematoporphyrin Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 electron donor ascorbic acid Corynebacterium diphtheriae biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 algal heme oxygenase requires a second reductant in addition to reduced pyridine nucleotide Cyanidium caldarium biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 electron donor NADPH, reductase: human or E. coli NADPH-cytochrome P450 reductase or putidaredoxin/putidaredoxin reductase Corynebacterium diphtheriae biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 NADH-dependent heme-degradation activity, 16% of NADH activity with 0.5 mM NADPH Bos taurus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 enzyme catalyzes oxidative cleavage of both heme b and heme c Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 enzyme catalyzes oxidative cleavage of both heme b and heme c Bos taurus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized Gallus gallus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized Homo sapiens biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized Sus scrofa biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized Bos taurus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 porphyrins without chelated iron and metalloporphyrins other than iron porphyrins are not oxidized Oryctolagus cuniculus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 intact cytochrome c is not oxidized Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 cytochrome c and myoglobin are not oxidized Bos taurus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 NADPH is more effective than NADH Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 electron donor NADPH Gallus gallus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 electron donor NADPH Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 electron donor NADPH Bos taurus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O - ? 287919 1.14.14.18 heme + electron donor + O2 - Mus musculus biliverdin + Fe2+ + CO + oxidized electron donor + H2O - ? 409569 1.14.14.18 heme + electron donor + O2 - Homo sapiens biliverdin + Fe2+ + CO + oxidized electron donor + H2O - ? 409569 1.14.14.18 heme + electron donor + O2 - Rattus norvegicus biliverdin + Fe2+ + CO + oxidized electron donor + H2O - ? 409569 1.14.14.18 heme + electron donor + O2 - Candida albicans biliverdin + Fe2+ + CO + oxidized electron donor + H2O - ? 409569 1.14.14.18 heme + ferredoxin + O2 HY1, HO3, and HO4 Arabidopsis thaliana biliverdin IXalpha + Fe2+ + CO + A + H2O - ? 409570 1.14.14.18 heme + NADH + O2 - Escherichia coli biliverdin + Fe2+ + CO + NAD+ + H2O - ? 388871 1.14.14.18 heme + NADH + O2 - Rattus norvegicus biliverdin + Fe2+ + CO + NAD+ + H2O - ? 388871 1.14.14.18 heme + NADPH + H+ + O2 - Glycine max biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O - ? 376936 1.14.14.18 heme + NADPH + H+ + O2 - Homo sapiens biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O wild-type, selective production of biliverdin IXalpha ? 376936 1.14.14.18 heme + NADPH + H+ + O2 - Homo sapiens biliverdin IXdelta + biliverdin IXalpha + Fe2+ + CO + NADP+ + H2O mutant R183E, yields about 20% of product biliverdin IXdelta ? 376937 1.14.14.18 heme + [reduced NADPH-hemoprotein reductase] + O2 - Leptospira interrogans serovar Icterohaemorrhagiae biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O - ? 443624 1.14.14.18 heme + [reduced NADPH-hemoprotein reductase] + O2 - Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601 biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O - ? 443624 1.14.14.18 heme c + NADPH + H+ + O2 - Bos taurus biliverdin c + Fe2+ + CO + NAD+ + H2O - r 451309 1.14.14.18 hemin + reduced acceptor + O2 - Rattus norvegicus alpha-meso-hydroxyhemin IX + CO + acceptor + H2O - ? 376938 1.14.14.18 methemoglobin + electron donor + O2 - Gallus gallus ? - ? 287920 1.14.14.18 methemoglobin + electron donor + O2 - Homo sapiens ? - ? 287920 1.14.14.18 methemoglobin + electron donor + O2 - Rattus norvegicus ? - ? 287920 1.14.14.18 methemoglobin + electron donor + O2 - Sus scrofa ? - ? 287920 1.14.14.18 methemoglobin + electron donor + O2 - Bos taurus ? - ? 287920 1.14.14.18 methemoglobin + electron donor + O2 - Oryctolagus cuniculus ? - ? 287920 1.14.14.18 methemoglobin + electron donor + O2 30% of activity with heme Rattus norvegicus ? - ? 287920 1.14.14.18 additional information involved in the control of wound healing Rattus norvegicus ? - ? 89 1.14.14.18 additional information reaction proceeds via three steps, first step is alpha-regioselective hydroxylation of hemin, second degradation of meso-hydroxyhemin to verdoheme and third degradation of verdoheme to biliverdin, which again is stereoselective for verdoheme IXalpha. In the second step, enzyme would convert all four isomers of meso-hydroxyhemin Rattus norvegicus ? - ? 89 1.14.14.18 additional information structure-function analysis Homo sapiens ? - ? 89 1.14.14.18 additional information butylated hydroxyanisole stimulates heme oxygenase-1 gene expression and inhibits neointima formation in rat arteries involving Nrf2 activation, overview Rattus norvegicus ? - ? 89 1.14.14.18 additional information capsaicin induces heme oxygenase-1 expression in Hep-G2 cells via activation of PI3K-Nrf2 signaling, and capsaicin protects against SIN-1-induced cytotoxicity, which is abolished by HO-1 inhibition Homo sapiens ? - ? 89 1.14.14.18 additional information expression and activity of heme oxygenase-1 is elevated in artificially induced low-flow priapism in rat penile tissues, overview Rattus norvegicus ? - ? 89 1.14.14.18 additional information expression of Hepatitis C virus core protein sensitizes hepatocytes to toxic injury and inhibits the induction of HO-1 in response to stress, overview Homo sapiens ? - ? 89 1.14.14.18 additional information heme oxygenase-1 inhibits breast cancer invasion via suppressing the expression of matrix metalloproteinase-9, overview Homo sapiens ? - ? 89 1.14.14.18 additional information heme oxygenase-1/CO pathway is a key modulator in NO-mediated antiapoptosis and anti-inflammation, mechanisms, overview, mechanisms for the HO-1-mediated inhibition of NO production, activation of the PI3K/Akt pathway, overview Homo sapiens ? - ? 89 1.14.14.18 additional information hemoglobin neurotoxicity is attenuated by inhibitors of the protein kinase CK2 and protein kinase C independent of heme oxygenase activity Mus musculus ? - ? 89 1.14.14.18 additional information HO-1 and its byproduct biliverdin play major roles in the pathophysiological cascade leading to renal I/R injury Rattus norvegicus ? - ? 89 1.14.14.18 additional information HO-1 gene regulation system, dynamic roles of transcriptional repressor BACH1 and transcription factor NRF2 in the transcription of the heme oxygenase-1 gene, overview Homo sapiens ? - ? 89 1.14.14.18 additional information HO-1 is involved in host defense reactions against various stresses, HO-1 modulates immunocyte activation and functions and suppresses mast cell degranulation, overview Rattus norvegicus ? - ? 89 1.14.14.18 additional information HO-1 is involved in the function of bax inhibitor-1, BI-1, an anti-apoptotic protein that is located in endoplasmic reticulum membranes and protects cells from endoplasmic reticulum stress-induced apoptosis. For BI-1 associated function, HO-1 expression is induced by nuclear factor erythroid 2-related factor 2, overview Homo sapiens ? - ? 89 1.14.14.18 additional information HO-1 protein delivery mediates activation of various transcription factors, nuclear localization of HO-1 has a signalling role, effect of nuclear localization of HO-1oncell viability, overview Rattus norvegicus ? - ? 89 1.14.14.18 additional information HO-1 regulation, HO-1 autoregulation, and HO-1 regulatory functions, activation of MAPK pathways is not required in HO-1 self-regulation, overview Rattus norvegicus ? - ? 89 1.14.14.18 additional information inhibition of heme oxygenase 1 expression by small interfering RNA decreases orthotopic tumor growth in livers of mice. Downmodulation of HO-1 by siRNA resulted in increased cellular damage and apoptosis, reduced proliferation, reduced growth of orthotopic hepatocellular carcinoma and reduced angiogenesis, mechanism, overview Mus musculus ? - ? 89 1.14.14.18 additional information inhibition of heme oxygenase-1 protects against tissue injury in carbon tetrachloride exposed livers, SnPP-IX-mediated HO-1 inhibition markedly aggravates intrahepatic leukocyte-endothelial cell interaction with an almost 2fold increase of the number of adherent leukocytes when compared with solely CCl4-exposed livers, overview Rattus norvegicus ? - ? 89 1.14.14.18 additional information LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview Mus musculus ? - ? 89 1.14.14.18 additional information NO derived from LPS-induced nitric oxide synthase, NOS, entails an increase in HO activity and this activity, in turn, is involved in the consequent inhibition of NOS, overview Rattus norvegicus ? - ? 89 1.14.14.18 additional information overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview Mus musculus ? - ? 89 1.14.14.18 additional information PMA-dependent activation of HO-1 is mediated via a nonclassical NF-kappaB pathway that is independent of IKK2 activity Mus musculus ? - ? 89 1.14.14.18 additional information PMA-dependent activation of HO-1 is mediated via a nonclassical NF-kappaB pathway that is independent of IKK2 activity Rattus norvegicus ? - ? 89 1.14.14.18 additional information the anti-inflammatory activity of Phellinus linteus is mediated through the PKCdelta/Nrf2/ARE signaling to up-regulation of heme oxygenase-1 Mus musculus ? - ? 89 1.14.14.18 additional information the enzyme activity is positively correlated with nitric oxide and cGMP levels in cavernous tissue, overview Rattus norvegicus ? - ? 89 1.14.14.18 additional information the enzyme has anti-inflammatory function in the vascular system via production of antioxidants bilirubin and biliverdin as well as CO, the enzyme contributes to cardiovascular health Homo sapiens ? - ? 89 1.14.14.18 additional information the enzyme is involved in cancer cell response to photodynamic therapy, overview Homo sapiens ? - ? 89 1.14.14.18 additional information ho-1 forms complexes with proteins from heavy metal-treated HeLa cells Homo sapiens ? - ? 89 1.14.14.18 additional information screening for heme proteins with heme oxygenase activity after de novo synthesis of the heme proteins on a membrane-coupled template, overview Bos taurus ? - ? 89 1.14.14.18 additional information a pattern of substrate methyl contact shifts that places the lone iron pi-spin in the dxz orbital, rather than the dyz orbital found in the cyanide complex. Low-spin, (dxy)2(dyz,dxz)3, ground state in both azide and cyanide complexes. Switch from singly occupied dyz for the cyanide to dxz for the azide complex of HO is consistent with the orbital hole determined by the azide pi-plane in the latter complex, which is ca. 90° in-plane rotated from that of the imidazole pi-plane Homo sapiens ? - ? 89 1.14.14.18 additional information ability of uncoupled HO-1 to produce large quantities of H2O2, H2O2 generation is much more efficient with the full-length form of HO-1 than with the soluble form Homo sapiens ? - ? 89 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 ? - ? 89 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 ? - ? 89 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 ? - ? 89 1.14.14.18 additional information heme oxygenase activity in rat spleen and brain microsomal fractions is determined by the quantitation of CO formed from the degradation of methemalbumin, i.e. heme complexed with albumin Rattus norvegicus ? - ? 89 1.14.14.18 additional information structure-function relationship and analysis, overview Homo sapiens ? - ? 89 1.14.14.18 additional information structure-function relationship and analysis, overview Corynebacterium diphtheriae ? - ? 89 1.14.14.18 additional information structure-function relationship and analysis, overview Rattus norvegicus ? - ? 89 1.14.14.18 additional information heme oxygenase activity in rat spleen and brain microsomal fractions is determined by the quantitation of CO formed from the degradation of methemalbumin, i.e. heme complexed with albumin Rattus norvegicus Sprague-Dawley ? - ? 89 1.14.14.18 additional information LPS-induced maturation of dendritic cells is dependent on STAT3 phosphorylation and independent of HO-1 activity, overview Mus musculus C57BL/6 ? - ? 89 1.14.14.18 additional information inhibition of heme oxygenase 1 expression by small interfering RNA decreases orthotopic tumor growth in livers of mice. Downmodulation of HO-1 by siRNA resulted in increased cellular damage and apoptosis, reduced proliferation, reduced growth of orthotopic hepatocellular carcinoma and reduced angiogenesis, mechanism, overview Mus musculus C3H/HEN ? - ? 89 1.14.14.18 protoheme + reduced acceptor + O2 + Fe2+ - Aedes aegypti biliverdin-IX-alpha + CO + Fe3+ + acceptor + H2O - ? 440381 1.14.14.18 protoheme + [reduced cytochrome P450 reductase] + O2 - Homo sapiens biliverdin + Fe2+ + CO + [oxidized cytochrome P450 reductase] + H2O - ? 443866 1.14.14.18 protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 - Homo sapiens biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O - ? 440384 1.14.14.18 protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 - Rattus norvegicus biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O - ? 440384 1.14.14.18 protoheme + [reduced NADPH-hemoprotein reductase] + H+ + O2 - Sus scrofa biliverdin-IX-alpha + CO + Fe2+ + [oxidized NADPH-hemoprotein reductase] + H2O - ? 440384 1.14.14.18 protoheme + [reduced NADPH-hemoprotein reductase] + O2 - Mus musculus biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O - ? 432916 1.14.14.18 protoheme + [reduced NADPH-hemoprotein reductase] + O2 - Homo sapiens biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O - ? 432916 1.14.14.18 protoheme + [reduced NADPH-hemoprotein reductase] + O2 - Rattus norvegicus biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O - ? 432916 1.14.14.18 protoheme + [reduced NADPH-hemoprotein reductase] + O2 - Corynebacterium diphtheriae biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O - ? 432916 1.14.14.18 protoheme + [reduced NADPH-hemoprotein reductase] + O2 - Pseudomonas aeruginosa biliverdin IXbeta + biliverdin IXdelta + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O - ? 443867 1.14.14.18 verdoheme IXalpha + H2O - Rattus norvegicus biliverdin IXalpha + Fe2+ - ? 378320