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Resonance raman studies of oxo intermediates in the reaction of pulsed cytochrome bo with hydrogen peroxide.

T Uchida1, T Mogi, T Kitagawa

  • 1Institute for Molecular Science, Okazaki National Research Institutes, Myodaiji, Okazaki 444-8585, Japan.

Biochemistry
|June 1, 2000
PubMed
Summary
This summary is machine-generated.

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Resonance Raman spectroscopy revealed key intermediates in Escherichia coli cytochrome bo function. The study identified an Fe(IV)=O heme and tyrosyl radical in the P intermediate, crucial for understanding oxygen reduction mechanisms.

Area of Science:

  • Biochemistry
  • Spectroscopy
  • Enzymology

Background:

  • Cytochrome bo from Escherichia coli is a heme-copper terminal oxidase.
  • It physiologically catalyzes O(2) reduction by quinols and proton translocation.
  • Understanding its reaction intermediates is vital for deciphering its mechanism.

Purpose of the Study:

  • To investigate the reaction of the ferric pulsed form of cytochrome bo with hydrogen peroxide.
  • To characterize the oxygen-isotope-sensitive Raman bands associated with reaction intermediates.
  • To elucidate the structural features of key intermediates, particularly the P and F species.

Main Methods:

  • Steady-state resonance Raman spectroscopy was employed.
  • A homemade microcirculating system was utilized for sample handling.

Related Experiment Videos

  • Oxygen isotope labeling (H(2)(16)O(2)/H(2)(18)O(2) and H(2)(16)O(18)O) was used to identify vibrational modes.

    • Main Results:

    • Three oxygen-isotope-sensitive Raman bands were observed at 805/X, 783/753, and (767)/730 cm(-1).
    • The 805/X cm(-1) band, increasing at higher pH, corresponds to the P intermediate, containing an Fe(IV)=O heme and a tyrosyl radical.
    • The 783/753 cm(-1) band, dominant at neutral pH, likely represents the F intermediate, while the (767)/730 cm(-1) species suggests a branched reaction pathway.

    Conclusions:

    • The P intermediate of cytochrome bo contains an Fe(IV)=O heme and a tyrosyl radical, similar to compound I of prostaglandin H synthase.
    • The F intermediate exhibits an oxoferryl species, analogous to bovine cytochrome c oxidase.
    • The presence of the (767)/730 cm(-1) species supports a branched reaction scheme for O(2) reduction by cytochrome bo.