Variation of the oxidation state of verdoheme in the heme oxygenase reaction

Biochemical and Biophysical Research Communications

Volumn 376, Issue 2, 2008, Pages 293-298

  Gohya, Tomohiko ^a   Sato, Michihiko ^b   Zhang, Xuhong ^b   Migita, Catharina T ^a  

^a YAMAGUCHI UNIVERSITY   (Japan)

^b YAMAGATA UNIVERSITY   (Japan)

Author keywords

Axial coordination structure; EPR; Heme degradation; Heme oxygenase; Oxidation state; Verdoheme

Indexed keywords

ALPHA HYDROXYHEMIN; BILIVERDIN; CARBON MONOXIDE; FERRIC BILIVERDIN DERIVATIVE; FERRIC ION; FERROUS ION; HEME DERIVATIVE; HEME OXYGENASE; HEME OXYGENASE 1; HEMIN; HYDROGEN PEROXIDE; IRON; ISOPROTEIN; UNCLASSIFIED DRUG; VERDOHEME;

ABSORPTION SPECTROSCOPY; ARTICLE; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; HUMAN; HUMAN CELL; HUMAN TISSUE; MOLECULAR STABILITY; OXIDATION; PRIORITY JOURNAL; PROTEIN VARIANT; REACTION ANALYSIS; SOYBEAN;

AMINO ACID SEQUENCE; ANIMALS; HEME; HEME OXYGENASE-1; HYDROGEN PEROXIDE; OXIDATION-REDUCTION; OXYGEN; PLANT PROTEINS; RATS; RECOMBINANT PROTEINS;

GLYCINE MAX; RATTUS;

EID: 52949098731     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.08.141     Document Type: Article

References (17)

1. Unno M., Matsui T., and Ikeda-Saito M. Structure and catalytic mechanism of heme oxygenase. Nat. Prod. Rep. 24 (2007) 553-570
2. Yoshida T., Noguchi M., and Kikuchi G. The step of carbon monoxide liberation in the sequence of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system. J. Biol. Chem. 257 (1982) 9345-9348
3. Gohya T., Zhang X., Yoshida T., and Migita C.T. Spectroscopic characterization of a higher plant heme oxygenase isoform-1 from Glycine max (soybean)-coordination structure of the heme complex and catabolism of heme. FEBS J. 273 (2006) 5384-5398
4. Wilks A., and Ortiz de Montellano P.R. Rat liver heme oxygenase: high level expression of a truncated soluble form and nature of the meso-hydroxylating species. J. Biol. Chem. 268 (1993) 22357-22362
5. 2-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation. J. Biol. Chem. 280 (2005) 36833-36840
6. Fujii H., Zhang X., Tomita T., Ikeda-Saito, and Yoshida T. A role for highly conserved carboxylate, aspartate-140, in oxygen activation and heme degradation by heme oxygenase-1;. J. Am. Chem. Soc. 123 (2001) 6475-6484
7. Mansfield Matera K., Zhou H., Migita C.T., Hobert S.E., Ishikawa K., Katakura K., Maeshima H., Yoshida T., and Ikeda-Saito M. Histidine-132 does not stabilize a distal water ligand and is not an important residue for the enzyme activity in heme oxygenase-1. Biochemistry 36 (1997) 4909-4915
8. Hase T., Mizutani S., and Mukohata Y. Expression of maize ferredoxin cDNA in Escherichia coli. Plant Physiol. 97 (1991) 1395-1401
9. + oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins. Plant Physiol. 123 (2000) 1037-1045
10. Migita C.T., Togashi S., Minakawa M., Zhang X., and Yoshida T. Evidence for the hydrophobic cavity of heme oxygenase-1 to be a CO-trapping site. Biochem. Biophys. Res. Commun. 338 (2005) 584-589
11. Migita C.T., Zhang X., and Yoshida T. Expression and characterization of cyanobacterium heme oxygenase, a key enzyme in the phycobilin synthesis, properties of the heme complex of recombinant active enzyme. Eur. J. Biochem. 270 (2003) 687-698
12. Liu Y., Moenne-Loccoz P., Loehr T.M., and Ortiz de Montellano P.R. Heme oxygenase-1, intermediates in verdoheme formation and the requirement for reducing equivalents. J. Biol. Chem. 272 (1997) 6909-6917
13. Migita C.T., Fujii H., Mansfield Matera K., Takahashi S., Zhou H., and Yoshida T. Molecular oxygen oxidizes the porphyrin ring of the ferric α-hydroxyheme in heme oxygenase in the presence of reducing equivalent. Biochim. Biophys. Acta 1432 (1999) 203-213
14. Mansfield Matera K., Takahashi S., Fujii H., Zhou H., Ishikawa K., Yoshimura K.T., Rousseau D.L., Yoshida T., and Ikeda-Saito M. Oxygen and one reducing equivalent are both required for the conversion of α-hydroxyhemin to verdoheme in heme oxygenase. J. Biol. Chem. 271 (1996) 6618-6624
15. Takahashi S., Mansfield Matera K., Fujii H., Zhou H., Ishikawa K., Yoshida T., Ikeda- Saito M., and Rousseau D.L. Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase. Biochemistry 36 (1997) 1402-1410
16. Damaso C.O., Bunce R.A., Barybin M.V., Wilks A., and Rivera M. The ferrous verdoheme-heme oxygenase complex is six-coordinate and low-spin. J. Am. Chem. Soc. 127 (2005) 17582-17583
17. Schuller D.J., Zhu W., Stojiljkovic I., Wilks A., and 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 (2001) 11552-11558