Nitrosyl cytochrome c oxidase. Formation and properties of mixed valence enzyme

Denis L. Rousseau, S. Singh, Y. C. Ching, M. Sassaroli

Research output: Contribution to journalArticle

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Abstract

We report the first resonance Raman scattering studies of NO-bound cytochrome c oxidase. Resonance Raman scattering and optical absorption spectra have been obtained on the fully reduced enzyme (a2+, a32+ NO) and the mixed valence enzyme (a3+, a32+ NO). Clear vibrational frequency shifts are detected in the lines associated with cytochrome a in comparing the two redox states. With 441.6 nm excitation the fully reduced preparation yields a spectrum similar to that of carbon monoxide-bound cytochrome c oxidase and is dominated by the spectrum of reduced cytochrome a. In contrast, in the mixed valence preparation no contributions from reduced cytochrome a are evident in the spectrum, verifying that this heme is no longer in the Fe2+ state. In the mixed valence NO-bound samples, a line appears at ~545 cm-1, a frequency similar to that found in NO-bound hemoglobin and myoglobin and assigned as an Fe-N-O-bending mode in those proteins. We do not detect this line in the spectrum of the fully reduced NO-bound enzyme. The carbonyl line of the cytochrome a3 heme formyl group in the fully reduced NO-bound enzyme appears at ≃1666 cm-1 in the resonance Raman spectrum. In the mixed valence NO-bound preparation the frequency of the carbonyl line increases by 1.2 cm-1 to ≃1667 cm-1. Thus, modes in cytochrome a32- NO are sensitive to the redox state of the cytochrome a and/or Cu(A) centers. We propose that the redox sensitivity of the formyl mode and the Fe-N-O mode results from an interaction between cytochrome a32+ (NO) and the cytochrome a-Cu(A) pair, and is linked to the cytochrome a3 (NO)) by the coupling between Cu(B) and the NO-bound cytochrome a3 heme.

Original languageEnglish (US)
Pages (from-to)5681-5685
Number of pages5
JournalJournal of Biological Chemistry
Volume263
Issue number12
StatePublished - 1988
Externally publishedYes

Fingerprint

Cytochromes a
Electron Transport Complex IV
Cytochromes a3
Heme
Oxidation-Reduction
Enzymes
Raman scattering
Raman Spectrum Analysis
Cytochromes
Myoglobin
Vibrational spectra
Carbon Monoxide
Light absorption
Absorption spectra
Hemoglobins
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Nitrosyl cytochrome c oxidase. Formation and properties of mixed valence enzyme. / Rousseau, Denis L.; Singh, S.; Ching, Y. C.; Sassaroli, M.

In: Journal of Biological Chemistry, Vol. 263, No. 12, 1988, p. 5681-5685.

Research output: Contribution to journalArticle

Rousseau, Denis L. ; Singh, S. ; Ching, Y. C. ; Sassaroli, M. / Nitrosyl cytochrome c oxidase. Formation and properties of mixed valence enzyme. In: Journal of Biological Chemistry. 1988 ; Vol. 263, No. 12. pp. 5681-5685.
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N2 - We report the first resonance Raman scattering studies of NO-bound cytochrome c oxidase. Resonance Raman scattering and optical absorption spectra have been obtained on the fully reduced enzyme (a2+, a32+ NO) and the mixed valence enzyme (a3+, a32+ NO). Clear vibrational frequency shifts are detected in the lines associated with cytochrome a in comparing the two redox states. With 441.6 nm excitation the fully reduced preparation yields a spectrum similar to that of carbon monoxide-bound cytochrome c oxidase and is dominated by the spectrum of reduced cytochrome a. In contrast, in the mixed valence preparation no contributions from reduced cytochrome a are evident in the spectrum, verifying that this heme is no longer in the Fe2+ state. In the mixed valence NO-bound samples, a line appears at ~545 cm-1, a frequency similar to that found in NO-bound hemoglobin and myoglobin and assigned as an Fe-N-O-bending mode in those proteins. We do not detect this line in the spectrum of the fully reduced NO-bound enzyme. The carbonyl line of the cytochrome a3 heme formyl group in the fully reduced NO-bound enzyme appears at ≃1666 cm-1 in the resonance Raman spectrum. In the mixed valence NO-bound preparation the frequency of the carbonyl line increases by 1.2 cm-1 to ≃1667 cm-1. Thus, modes in cytochrome a32- NO are sensitive to the redox state of the cytochrome a and/or Cu(A) centers. We propose that the redox sensitivity of the formyl mode and the Fe-N-O mode results from an interaction between cytochrome a32+ (NO) and the cytochrome a-Cu(A) pair, and is linked to the cytochrome a3 (NO)) by the coupling between Cu(B) and the NO-bound cytochrome a3 heme.

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