PMID- 10828985
OWN - NLM
STAT- MEDLINE
DCOM- 20000710
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 39
IP  - 22
DP  - 2000 Jun 6
TI  - Resonance raman studies of oxo intermediates in the reaction of pulsed cytochrome 
      bo with hydrogen peroxide.
PG  - 6669-78
AB  - Cytochrome bo from Escherichia coli, a member of the heme-copper terminal oxidase 
      superfamily, physiologically catalyzes reduction of O(2) by quinols and 
      simultaneously translocates protons across the cytoplasmic membrane. The reaction 
      of its ferric pulsed form with hydrogen peroxide was investigated with 
      steady-state resonance Raman spectroscopy using a homemade microcirculating 
      system. Three oxygen-isotope-sensitive Raman bands were observed at 805/X, 
      783/753, and (767)/730 cm(-)(1) for intermediates derived from 
      H(2)(16)O(2)/H(2)(18)O(2). The experiments using H(2)(16)O(18)O yielded no new 
      bands, indicating that all the bands arose from the Fe=O stretching 
      (nu(Fe)(=)(O)) mode. Among them, the intensity of the 805/X cm(-)(1) pair 
      increased at higher pH, and the species giving rise to this band seemed to 
      correspond to the P intermediate of bovine cytochrome c oxidase (CcO) on the 
      basis of the reported fact that the P intermediate of cytochrome bo appeared 
      prior to the formation of the F species at higher pH. For this intermediate, a 
      Raman band assignable to the C-O stretching mode of a tyrosyl radical was deduced 
      at 1489 cm(-)(1) from difference spectra. This suggests that the P intermediate 
      of cytochrome bo contains an Fe(IV)=O heme and a tyrosyl radical like compound I 
      of prostaglandin H synthase. The 783/753 cm(-)(1) pair, which was dominant at 
      neutral pH and close to the nu(Fe)(=)(O) frequency of the oxoferryl intermediate 
      of CcO, presumably arises from the F intermediate. On the contrary, the (767)/730 
      cm(-)(1) species has no counterpart in CcO. Its presence may support the branched 
      reaction scheme proposed previously for O(2) reduction by cytochrome bo.
FAU - Uchida, T
AU  - Uchida T
AD  - Institute for Molecular Science, Okazaki National Research Institutes, Myodaiji, 
      Okazaki 444-8585, Japan.
FAU - Mogi, T
AU  - Mogi T
FAU - Kitagawa, T
AU  - Kitagawa T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Bacterial Proteins)
RN  - 0 (Cytochrome b Group)
RN  - 0 (Cytochromes)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Free Radicals)
RN  - 0 (Oxygen Isotopes)
RN  - 42HK56048U (Tyrosine)
RN  - 42VZT0U6YR (Heme)
RN  - 7U1EE4V452 (Carbon Monoxide)
RN  - 9035-48-7 (cytochrome bo, E coli)
RN  - BBX060AN9V (Hydrogen Peroxide)
RN  - E1UOL152H7 (Iron)
RN  - J65BV539M3 (Deuterium Oxide)
SB  - IM
MH  - Bacterial Proteins/*chemistry
MH  - Carbon Monoxide/chemistry
MH  - *Cytochrome b Group
MH  - Cytochromes/*chemistry
MH  - Deuterium Oxide
MH  - Escherichia coli
MH  - *Escherichia coli Proteins
MH  - Free Radicals
MH  - Heme/chemistry
MH  - Hydrogen Peroxide/*chemistry
MH  - Hydrogen-Ion Concentration
MH  - Iron/chemistry
MH  - Oxygen Isotopes
MH  - Spectrum Analysis, Raman
MH  - Tyrosine/chemistry
EDAT- 2000/06/01 09:00
MHDA- 2000/07/15 11:00
CRDT- 2000/06/01 09:00
PHST- 2000/06/01 09:00 [pubmed]
PHST- 2000/07/15 11:00 [medline]
PHST- 2000/06/01 09:00 [entrez]
AID - bi992538r [pii]
AID - 10.1021/bi992538r [doi]
PST - ppublish
SO  - Biochemistry. 2000 Jun 6;39(22):6669-78. doi: 10.1021/bi992538r.