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References
Maines, M.D.; Ibrahim, N.G.; Kappas, A.: Solubilization and partial purification of heme oxygenase from rat liver. J. Biol. Chem., 252, 5900–5903 (1977)
Schacter, B.A.: Assay of microsomal heme oxygenase in liver and spleen. Methods Enzymol, 52, 367–372 (1978) 270
Bonkovsky, H.L.; Healy, J.F.; Pohl, J.: Purification and characterization of heme oxygenase from chick liver. Comparison of the avian and mammalian enzymes. Eur. J. Biochem., 189, 155–160 (1990)
Yoshinaga, T.; Sudo, Y.; Sano, S.: Enzymic conversion of α-oxyprotohaem IX into biliverdin IX α by haem oxygenase. Biochem. J., 270, 659–664 (1990)
Frydman, R.B.; Tomaro, M.L.; Buldain, G.; Awruch, J.; Diaz, L.; Frydman, B.: Specificity of heme oxygenase: a study with synthetic hemins. Biochemistry, 20, 5177–5182 (1981)
Tomaro, M.L.; Frydman, R.B.; Frydman, B.; Pandey, R.K.; Smith, K.M.: The oxidation of hemins by microsomal heme oxygenase. Structural requirements for the retention of substrate activity. Biochim. Biophys. Acta, 791, 342–349 (1984)
Maines, M.D.; Kappas, A.: Enzymatic oxidation of cobalt protoporphyrin IX: observations on the mechanism of heme oxygenase action. Biochemistry, 16, 419–423 (1977)
Kutty, R.K.; Maines, M.D.: Oxidation of heme c derivatives by purified heme oxygenase. Evidence for the presence of one molecular species of heme oxygenase in the rat liver. J. Biol. Chem., 257, 9944–9952 (1982)
Yoshida, T.; Kikuchi, G.: Purification and properties of heme oxygenase from pig spleen microsomes. J. Biol. Chem., 253, 4224–4229 (1978)
Matasek, P.; Solangi, K.; Goodman, A.I.; Levere, R.D.; Chernick, R.J.; Abraham, N.G.: Properties of human kidney heme oxygenase: inhibition by synthetic heme analogues and metalloporphyrins. Biochem. Biophys. Res. Commun., 157, 480–487 (1988)
Yoshinaga, T.; Sassa, S.; Kappas, A.: Purification and properties of bovine spleen heme oxygenase. Amino acid composition and sites of action of inhibitors of heme oxidation. J. Biol. Chem., 257, 7778–7785 (1982)
Trakshel, G.M.; Kutty, R.K.; Maines, M.D.: Purification and characterization of the major constitutive form of testicular heme oxygenase. The noninducible isoform. J. Biol. Chem., 261, 11131–11137 (1986)
Cornejo, J.; Beale, S.I.: Algal heme oxygenase from Cyanidium caldarium. Partial purification and fractionation into three required protein components. J. Biol. Chem., 263, 11915–11921 (1988)
Trakshel, G.M.; Maines, M.D.: Multiplicity of heme oxygenase isozymes. HO-1 and HO-2 are different molecular species in rat and rabbit. J. Biol. Chem., 264, 1323–1328 (1989)
Kutty, R.K.; Maines, M.D.: Characterization of an NADH-dependent haemdegrading system in ox heart mitochondria. Biochem. J., 246, 467–474 (1987)
Braggins, P.E.; Trakshel, G.M.; Kutty, R.K.; Maines, M.D.: Characterization of two heme oxygenase isoforms in rat spleen: comparison with the hematin-induced and constitutive isoforms of the liver. Biochem. Biophys. Res. Commun., 141, 528–533 (1986)
Rosenberg, D.W.; Kappas, A.: Characterization of heme oxygenase in the small intestinal epithelium. Arch. Biochem. Biophys., 274, 471–480 (1989)
Yoshida, T.; Kikuchi, G.: Purification and properties of heme oxygenase from rat liver microsomes. J. Biol. Chem., 254, 4487–4491 (1979)
Yoshinaga, T.; Sassa, S.; Kappas, A.: The oxidative degradation of heme c by the microsomal heme oxygenase system. J. Biol. Chem., 257, 7803–7807 (1982)
Rhie, G.E.; Beale, S.I.: Regulation of heme oxygenase activity in Cyanidium caldarium by light, glucose, and phycobilin precursors. J. Biol. Chem., 269, 9620–9626 (1994)
Ishikawa, K.; Takeuchi, N.; Takahashi, S.; Matera, K.M.; Sato, M.; Shibahara, S.; Rousseau, D.L.; Ikeda-Saito, M.; Yoshida, T.: Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2. J. Biol. Chem., 270, 6345–6350 (1995)
Wilks, A.; Black, S.M.; Miller, W.L.; Ortiz de Montellano, P.R.: Expression and characterization of truncated human heme oxygenase (hHO-1) and a fusion protein of hHO-1 with human cytochrome P450 reductase. Biochemistry, 34, 4421–4427 (1995)
Wilks, A.; de Montellano, P.R.O.; Sun, J.; Loehr, T.M.: Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis. Biochemistry, 35, 930–936 (1996)
Torpey, J.; Ortiz de Montellano, P.R.: Oxidation of α-meso-formylmesoheme by heme oxygenase. Electronic control of the reaction regiospecificity. J. Biol. Chem., 272, 22008–22014 (1997)
Wilks, A.; Schmitt, M.P.: Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocyle. J. Biol. Chem., 273, 837–841 (1998)
Chu, G.C.; Katakura, K.; Zhang, X.; Yoshida, T.; Ikeda-Saito, M.: Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae. J. Biol. Chem., 274, 21319–21325 (1999)
Schuller, D.J.; Wilks, A.; De Montellano, P.R.O.; Poulos, T.L.: Crystal structure of human heme oxygenase-1. Nat. Struct. Biol., 6, 860–867 (1999)
Ding, Y.; McCoubrey, W.K., Jr.; Maines, M.D.: Interaction of heme oxygenase-2 with nitric oxide donors: is the oxygenase an intracellular sink for NO?. Eur. J. Biochem., 264, 854–861 (1999)
Wilks, A.; Moenne-Loccoz, P.: Identification of the proximal ligand His-20 in heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Oxidative cleavage of the heme macrocycle does not require the proximal histidine. J. Biol. Chem., 275, 11686–11692 (2000)
Liu, Y.; Ortiz de Montellano, PR.: Reaction intermediates and single turn-over rate constants for the oxidation of heme by human heme oxygenase-1. J. Biol. Chem., 275, 5297–5307 (2000)
Zhou, H.; Migita, C.T.; Sato, M.; Sun, D.; Zhang, X.; Ikeda-Saito, M.; Fujii, H.; Yoshida, T.: Participation of carboxylate amino acid side chain in regiospecific oxidation of heme by heme oxygenase. J. Am. Chem. Soc, 122, 8311–8312 (2000)
Botros, F.T.; Laniado-Schwartzmann, M.; Abraham, N.G.: Regulation of cyclooxygenase-and cytochrome P450-derived eicosanoids by heme oxygenase in the rat kidney. Hypertension, 39, 639–644 (2002)
Christova, T.Y.; Duridanova, D.B.; Setchenska, M.S.: Enhanced heme oxygenase activity increases the antioxidant defense capacity of guinea pig liver upon acute cobalt chloride loading: comparison with rat liver. Comp. Biochem. Physiol. C, 131, 177–184 (2002)
Ryter, S.W.; Otterbein, L.E.; Morse, D.; Choi, A.M.K.: Heme oxygenase/carbon monoxide signaling pathways: Regulation and functional significance. Mol. Cell. Biochem., 234-235, 249–263 (2002)
Sugishima, M.; Sakamoto, H.; Higashimoto, Y.; Omata, Y.; Hayashi, S.; Noguchi, M.; Fukuyama, K.: Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide. Implication for regiospecific hydroxylation of heme at the α-meso carbon. J. Biol. Chem., 277, 45086–45090 (2002)
Davydov, R.; Kofman, V.; Fujii, H.; Yoshida, T.; Ikeda-Saito, M.; Hoffman, B.M.: Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants. J. Am. Chem. Soc, 124, 1798–1808 (2002)
Schuller, D.J.; Zhu, W.; Stojiljkovic, I.; Wilks, A.; Poulos, T.L.: Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1. Biochemistry, 40, 11552–11558 (2001)
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(2006). Heme oxygenase (decyclizing). In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 27. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-30439-8_30
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DOI: https://doi.org/10.1007/3-540-30439-8_30
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