PMID- 23723073
OWN - NLM
STAT- MEDLINE
DCOM- 20130927
LR  - 20211021
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 288
IP  - 28
DP  - 2013 Jul 12
TI  - The protein effect in the structure of two ferryl-oxo intermediates at the same 
      oxidation level in the heme copper binuclear center of cytochrome c oxidase.
PG  - 20261-6
LID - 10.1074/jbc.M113.468488 [doi]
AB  - Identification of the intermediates and determination of their structures in the 
      reduction of dioxygen to water by cytochrome c oxidase (CcO) are particularly 
      important to understanding both O2 activation and proton pumping by the enzyme. 
      In this work, we report the products of the rapid reaction of O2 with the mixed 
      valence form (CuA(2+), heme a(3+), heme a3(2+)-CuB(1+)) of the enzyme. The 
      resonance Raman results show the formation of two ferryl-oxo species with 
      characteristic Fe(IV)=O stretching modes at 790 and 804 cm(-1) at the peroxy 
      oxidation level (PM). Density functional theory calculations show that the 
      protein environment of the proximal H-bonded His-411 determines the strength of 
      the distal Fe(IV)=O bond. In contrast to previous proposals, the PM intermediate 
      is also formed in the reaction of Y167F with O2. These results suggest that in 
      the fully reduced enzyme, the proton pumping nu(Fe(IV)=O) = 804 cm(-1) to 
      nu(Fe(IV)=O) = 790 cm(-1) transition (P-->F, where P is peroxy and F is ferryl) is 
      triggered not only by electron transfer from heme a to heme a3 but also by the 
      formation of the H-bonded form of the His-411-Fe(IV)=O conformer in the proximal 
      site of heme a3. The implications of these results with respect to the role of an 
      O=Fe(IV)-His-411-H-bonded form to the ring A propionate of heme a3-Asp-399-H2O 
      site and, thus, to the exit/output proton channel (H2O) pool during the proton 
      pumping P-->F transition are discussed. We propose that the environment proximal to 
      the heme a3 controls the spectroscopic properties of the ferryl intermediates in 
      cytochrome oxidases.
FAU - Pinakoulaki, Eftychia
AU  - Pinakoulaki E
AD  - Department of Chemistry, University of Cyprus, P. O. Box 20537, 1678 Nicosia, 
      Cyprus.
FAU - Daskalakis, Vangelis
AU  - Daskalakis V
FAU - Ohta, Takehiro
AU  - Ohta T
FAU - Richter, Oliver-Matthias H
AU  - Richter OM
FAU - Budiman, Kerstin
AU  - Budiman K
FAU - Kitagawa, Teizo
AU  - Kitagawa T
FAU - Ludwig, Bernd
AU  - Ludwig B
FAU - Varotsis, Constantinos
AU  - Varotsis C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130530
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Bacterial Proteins)
RN  - 0 (Oxygen Isotopes)
RN  - 0 (Peroxides)
RN  - 42VZT0U6YR (Heme)
RN  - 4QD397987E (Histidine)
RN  - 789U1901C5 (Copper)
RN  - E1UOL152H7 (Iron)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Bacterial Proteins/*chemistry/metabolism
MH  - Copper/*chemistry/metabolism
MH  - Electron Transport Complex IV/*chemistry/metabolism
MH  - Heme/*chemistry/metabolism
MH  - Histidine/chemistry/metabolism
MH  - Hydrogen Bonding
MH  - Iron/*chemistry/metabolism
MH  - Oxidation-Reduction
MH  - Oxygen/*chemistry/metabolism
MH  - Oxygen Isotopes
MH  - Paracoccus denitrificans/enzymology
MH  - Peroxides/chemistry/metabolism
MH  - Spectrum Analysis, Raman
PMC - PMC3711293
OTO - NOTNLM
OT  - Bioenergetics
OT  - Computation
OT  - Cytochrome Oxidase
OT  - Heme
OT  - Raman Spectroscopy
EDAT- 2013/06/01 06:00
MHDA- 2013/09/28 06:00
PMCR- 2014/07/12
CRDT- 2013/06/01 06:00
PHST- 2013/06/01 06:00 [entrez]
PHST- 2013/06/01 06:00 [pubmed]
PHST- 2013/09/28 06:00 [medline]
PHST- 2014/07/12 00:00 [pmc-release]
AID - S0021-9258(20)45597-8 [pii]
AID - M113.468488 [pii]
AID - 10.1074/jbc.M113.468488 [doi]
PST - ppublish
SO  - J Biol Chem. 2013 Jul 12;288(28):20261-6. doi: 10.1074/jbc.M113.468488. Epub 2013 
      May 30.