Two conformations of the catalytic site in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides

J. Wang, S. Takahashi, J. P. Hosler, D. M. Mitchell, S. Ferguson-Miller, R. B. Gennis, Denis L. Rousseau

Research output: Contribution to journalArticle

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Abstract

Resonance Raman spectra of the carbon monoxy derivative of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides show two distinct Fe-CO stretching modes (519 and 493 cm-1) at room temperature. The frequency of the mode at 519 cm-1 coincides with that of other terminal oxidases at neutral pH. Two C-O stretching modes, one at 1966 cm-1 and one at 1955 cm- 1, are also found. The splitting of the C-O stretching mode is consistent with the FTIR spectra of cytochrome c oxidases at cryogenic temperatures in which two different conformations (α and β) of the catalytic site of the enzyme are present. The splitting of both the Fe-CO and C-O stretching modes under our conditions indicates that these two forms of the enzyme are also present at room temperature, and with the additional information on the Fe- CO modes provided here, a structural origin for the two forms may be postulated. The α-form has the same general structure of the active site as mammalian oxidase, a structure in which the copper atom that is the part of the Fe-Cu(B) binuclear site interacts strongly with the bound CO. We postulate that the copper atom exerts a strong polar or steric effect on the heme-bound CO, resulting in either compression of the Fe-CO bond or distortion of the Fe-CO moiety. On the other hand, the β-form has an open structure typical of heme proteins with histidine coordination to the iron trans to a Fe-C-O moiety where there is no interaction with a copper atom in the distal pocket. The functional significance of these two forms of the enzyme remains to be determined.

Original languageEnglish (US)
Pages (from-to)9819-9825
Number of pages7
JournalBiochemistry
Volume34
Issue number31
DOIs
StatePublished - 1995
Externally publishedYes

Fingerprint

Rhodobacter sphaeroides
Electron Transport Complex IV
Carbon Monoxide
Conformations
Catalytic Domain
Stretching
Copper
Atoms
Temperature
Oxidoreductases
Enzymes
Hemeproteins
Fourier Transform Infrared Spectroscopy
Heme
Histidine
Cryogenics
Raman scattering
Carbon
Iron
Derivatives

ASJC Scopus subject areas

  • Biochemistry

Cite this

Wang, J., Takahashi, S., Hosler, J. P., Mitchell, D. M., Ferguson-Miller, S., Gennis, R. B., & Rousseau, D. L. (1995). Two conformations of the catalytic site in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry, 34(31), 9819-9825. https://doi.org/10.1021/bi00031a001

Two conformations of the catalytic site in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides. / Wang, J.; Takahashi, S.; Hosler, J. P.; Mitchell, D. M.; Ferguson-Miller, S.; Gennis, R. B.; Rousseau, Denis L.

In: Biochemistry, Vol. 34, No. 31, 1995, p. 9819-9825.

Research output: Contribution to journalArticle

Wang, J, Takahashi, S, Hosler, JP, Mitchell, DM, Ferguson-Miller, S, Gennis, RB & Rousseau, DL 1995, 'Two conformations of the catalytic site in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides', Biochemistry, vol. 34, no. 31, pp. 9819-9825. https://doi.org/10.1021/bi00031a001
Wang J, Takahashi S, Hosler JP, Mitchell DM, Ferguson-Miller S, Gennis RB et al. Two conformations of the catalytic site in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides. Biochemistry. 1995;34(31):9819-9825. https://doi.org/10.1021/bi00031a001
Wang, J. ; Takahashi, S. ; Hosler, J. P. ; Mitchell, D. M. ; Ferguson-Miller, S. ; Gennis, R. B. ; Rousseau, Denis L. / Two conformations of the catalytic site in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides. In: Biochemistry. 1995 ; Vol. 34, No. 31. pp. 9819-9825.
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