PMID- 11132644
OWN - NLM
STAT- MEDLINE
DCOM- 20010329
LR  - 20190910
IS  - 0162-0134 (Print)
IS  - 0162-0134 (Linking)
VI  - 82
IP  - 1-4
DP  - 2000 Nov
TI  - Structures of reaction intermediates of bovine cytochrome c oxidase probed by 
      time-resolved vibrational spectroscopy.
PG  - 9-18
AB  - Structures of reaction intermediates of bovine cytochrome c oxidase (CcO) in the 
      reactions of its fully reduced form with O2 and fully oxidized form with H2O2 
      were investigated with time-resolved resonance Raman (RR) and infrared 
      spectroscopy. Six oxygen-associated RR bands were observed for the reaction of 
      CcO with O2. The isotope shifts for an asymmetrically labeled dioxygen, 
      (16)O(18)O, has established that the primary intermediate of cytochrome a3 is an 
      end-on type dioxygen adduct and the subsequent intermediate (P) is an oxoiron 
      species with Fe=O stretch (nu(Fe=O)) at 804/764 cm(-1) for (16)O2/(18)O2 
      derivatives, although it had been long postulated to be a peroxy species. The P 
      intermediate is converted to the F intermediate with nu(Fe=O) at 785/751 cm(-1) 
      and then to a ferric hydroxy species with nu(Fe-OH) at 450/425 cm(-1) (443/417 
      cm(-1) in D2O). The rate of reaction from P to F intermediates is significantly 
      slower in D2O than in H2O. The reaction of oxidized CcO with H2O2 yields the same 
      oxygen isotope-sensitive bands as those of P and F, indicating the identity of 
      intermediates. Time-resolved infrared spectroscopy revealed that deprotonation of 
      carboxylic acid side chain takes place upon deligation of a ligand from heme a3. 
      UV RR spectrum gave a prominent band due to cis C=C stretch of phospholipids 
      tightly bound to purified CcO.
FAU - Kitagawa, T
AU  - Kitagawa T
AD  - Center for Integrative Bioscience, Okazaki National Research Institutes, 
      Myodaiji, Japan. teizo@ims.ac.jp
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - United States
TA  - J Inorg Biochem
JT  - Journal of inorganic biochemistry
JID - 7905788
RN  - 0 (Amino Acids)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Amino Acids/chemistry
MH  - Animals
MH  - Cattle
MH  - Electron Transport Complex IV/*chemistry/metabolism
MH  - Mitochondria/*enzymology
MH  - Models, Biological
MH  - Oxidation-Reduction
MH  - Oxygen/chemistry
MH  - Spectroscopy, Fourier Transform Infrared
MH  - Spectrum Analysis, Raman
RF  - 37
EDAT- 2001/01/02 11:00
MHDA- 2001/04/03 10:01
CRDT- 2001/01/02 11:00
PHST- 2001/01/02 11:00 [pubmed]
PHST- 2001/04/03 10:01 [medline]
PHST- 2001/01/02 11:00 [entrez]
AID - S0162-0134(00)00155-0 [pii]
AID - 10.1016/s0162-0134(00)00155-0 [doi]
PST - ppublish
SO  - J Inorg Biochem. 2000 Nov;82(1-4):9-18. doi: 10.1016/s0162-0134(00)00155-0.