Probing the oxygen activation reaction in intact whole mitochondria through analysis of molecular vibrations

Toshinari Takahashi, Shigeki Kuroiwa, Takashi Ogura, Shinya Yoshikawa

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The process of dioxygen reduction catalyzed by cytochrome c oxidase was investigated by examining intact porcine mitochondrial preparations using a novel time-resolved resonance Raman measurement system at experimental accuracy levels equivalent to those of the reaction system of the solubilized and purified enzyme. The resonance Raman bands assignable to the initial three intermediates were detected at frequencies identical to those observed with purified enzyme preparations. However, the lifetime of the initial intermediate (the oxygenated species) in the mitochondrial preparation was found to be significantly longer than that observed in purified preparations, suggesting that control of the stability of the oxygenated species is imposed by the mitochondrial membrane system.

Original languageEnglish
Pages (from-to)9970-9971
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number28
DOIs
Publication statusPublished - 2005 Jul 20
Externally publishedYes

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Molecular vibrations
Mitochondria
Vibration
Enzymes
Chemical activation
Oxygen
Mitochondrial Membranes
Electron Transport Complex IV
Swine
Membranes

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Probing the oxygen activation reaction in intact whole mitochondria through analysis of molecular vibrations. / Takahashi, Toshinari; Kuroiwa, Shigeki; Ogura, Takashi; Yoshikawa, Shinya.

In: Journal of the American Chemical Society, Vol. 127, No. 28, 20.07.2005, p. 9970-9971.

Research output: Contribution to journalArticle

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