Oxygen-bound heme-heme oxygenase complex: Evidence for a highly bent structure of the coordinated oxygen

Satoshi Takahashi, Denis L. Rousseau, Noriko Takeuchi, Masao Ikeda-Saito, Tadashi Yoshida, Denis L. Rousseau

Research output: Contribution to journalArticle

95 Citations (Scopus)

Abstract

Heme oxygenase is the first and rate limiting enzyme of the microsomal heme degradation pathway. Heme (iron protoporphyrin-IX), a co-factor and substrate of the enzyme, is catabolized through a process in which the key step involves the hydroxylation of the α-meso carbon of the porphyrin macrocycle by heme-bound oxygen. To study the mechanism of this reaction, we have formed the metastable O2 adduct of the heme-heme oxygenase complex and observed that its resonance Raman spectrum displays an oxygen isotope shift pattern unlike those of any other O2-bound heme proteins. Analysis of the spectra suggests that the Fe-O-O unit is highly bent, showing that steric interactions between the bound O2 and the residues of the distal pocket result in a unique mechanism of oxygen activation. We propose that the terminal oxygen atom is in van der Waals contact with an α-meso carbon of the porphyrin ring.

Original languageEnglish (US)
Pages (from-to)6002-6006
Number of pages5
JournalJournal of the American Chemical Society
Volume117
Issue number22
StatePublished - Jun 7 1995
Externally publishedYes

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Heme Oxygenase (Decyclizing)
Heme
Oxygen
Porphyrins
Carbon
Oxygen Isotopes
Enzymes
Hemeproteins
Hydroxylation
Isotopes
Raman scattering
Spectrum Analysis
Chemical activation
Iron
Degradation
Atoms
Oxygenases
Substrates

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Takahashi, S., Rousseau, D. L., Takeuchi, N., Ikeda-Saito, M., Yoshida, T., & Rousseau, D. L. (1995). Oxygen-bound heme-heme oxygenase complex: Evidence for a highly bent structure of the coordinated oxygen. Journal of the American Chemical Society, 117(22), 6002-6006.

Oxygen-bound heme-heme oxygenase complex : Evidence for a highly bent structure of the coordinated oxygen. / Takahashi, Satoshi; Rousseau, Denis L.; Takeuchi, Noriko; Ikeda-Saito, Masao; Yoshida, Tadashi; Rousseau, Denis L.

In: Journal of the American Chemical Society, Vol. 117, No. 22, 07.06.1995, p. 6002-6006.

Research output: Contribution to journalArticle

Takahashi, S, Rousseau, DL, Takeuchi, N, Ikeda-Saito, M, Yoshida, T & Rousseau, DL 1995, 'Oxygen-bound heme-heme oxygenase complex: Evidence for a highly bent structure of the coordinated oxygen', Journal of the American Chemical Society, vol. 117, no. 22, pp. 6002-6006.
Takahashi, Satoshi ; Rousseau, Denis L. ; Takeuchi, Noriko ; Ikeda-Saito, Masao ; Yoshida, Tadashi ; Rousseau, Denis L. / Oxygen-bound heme-heme oxygenase complex : Evidence for a highly bent structure of the coordinated oxygen. In: Journal of the American Chemical Society. 1995 ; Vol. 117, No. 22. pp. 6002-6006.
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