PMID- 8555201
OWN - NLM
STAT- MEDLINE
DCOM- 19960227
LR  - 20131121
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 35
IP  - 1
DP  - 1996 Jan 9
TI  - Microcirculating system for simultaneous determination of Raman and absorption 
      spectra of enzymatic reaction intermediates and its application to the reaction 
      of cytochrome c oxidase with hydrogen peroxide.
PG  - 76-82
AB  - A new high-performance device for Raman/absorption simultaneous determination was 
      developed. This was combined with a newly designed microcirculating system and 
      was successfully applied to study intermediates in the reaction of bovine 
      oxidized cytochrome c oxidase (CcO) with hydrogen peroxide under steady state 
      conditions at ambient temperatures. Measurements with this device made it 
      possible to correlate directly the species defined in terms of the visible 
      absorption characteristics with specific Raman bands. The "607 nm" form of the 
      enzyme obtained with H2(16)O2 gave an oxygen isotope sensitive band at 804 cm-1 
      (769 cm-1 with H2(18)O2) in the Soret excited resonance Raman (RR) spectrum. Its 
      frequency and isotope frequency shifts are exactly the same as those observed 
      previously with 607 nm excitation in nonsimultaneous measurements for the 607 nm 
      form, for which the presence of an oxoiron heme was demonstrated. The so-called " 
      580 nm" form of the enzyme obtained with H2(16)O2 gave the main oxygen isotope 
      sensitive band at 785 cm-1 (750 cm-1 with H2(18)O2) but appeared to consist of 
      multiple species. This band was assigned to the FeIV = O stretching mode of 
      ferryloxo heme on the basis of its isotopic frequency shift. Another oxygen 
      isotope sensitive band was found at 355 cm-1 (340 cm-1 for H2(18)O2), similar to 
      the case of dioxygen reaction. Temporal behavior of this band did not agree with 
      either that of the 804 cm-1 band or that of the 785 cm-1 band but seemed to grow 
      between the two species. The RR spectra in the higher frequency region of the 607 
      nm and 580 nm forms excited at 427 nm were quite alike and did not support the 
      formation of a porphyrin pi-cation radical.
FAU - Proshlyakov, D A
AU  - Proshlyakov DA
AD  - Graduate University for Advanced Studies, Okazaki National Research Institutes, 
      Japan.
FAU - Ogura, T
AU  - Ogura T
FAU - Shinzawa-Itoh, K
AU  - Shinzawa-Itoh K
FAU - Yoshikawa, S
AU  - Yoshikawa S
FAU - Kitagawa, T
AU  - Kitagawa T
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Oxygen Isotopes)
RN  - BBX060AN9V (Hydrogen Peroxide)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Animals
MH  - Cattle
MH  - Electron Transport Complex IV/*chemistry/*metabolism
MH  - Hydrogen Peroxide/*metabolism
MH  - Kinetics
MH  - Oxidation-Reduction
MH  - Oxygen
MH  - Oxygen Isotopes
MH  - Spectrophotometry/*instrumentation/methods
MH  - Spectrum Analysis, Raman/*instrumentation/methods
EDAT- 1996/01/09 00:00
MHDA- 1996/01/09 00:01
CRDT- 1996/01/09 00:00
PHST- 1996/01/09 00:00 [pubmed]
PHST- 1996/01/09 00:01 [medline]
PHST- 1996/01/09 00:00 [entrez]
AID - bi9511705 [pii]
AID - 10.1021/bi9511705 [doi]
PST - ppublish
SO  - Biochemistry. 1996 Jan 9;35(1):76-82. doi: 10.1021/bi9511705.