PMID- 21795816
OWN - NLM
STAT- MEDLINE
DCOM- 20111026
LR  - 20131121
IS  - 1399-0047 (Electronic)
IS  - 0907-4449 (Linking)
VI  - 67
IP  - Pt 8
DP  - 2011 Aug
TI  - Distinguishing between Cl- and O2(2-) as the bridging element between Fe3+ and 
      Cu2+ in resting-oxidized cytochrome c oxidase.
PG  - 742-4
LID - 10.1107/S0907444911022803 [doi]
AB  - Fully oxidized cytochrome c oxidase (CcO) under enzymatic turnover is capable of 
      pumping protons, while fully oxidized CcO as isolated is not able to do so upon 
      one-electron reduction. The functional difference is expected to be a consequence 
      of structural differences: [Fe(3+)-OH(-)] under enzymatic turnover versus 
      [Fe(3+)-O(2)(2-)-Cu(2+)] for the as-isolated CcO. However, the electron density 
      for O(2)(2-) is equally assignable to Cl(-). An anomalous dispersion analysis was 
      performed in order to conclusively demonstrate the absence of Cl(-) between the 
      Fe(3+) and Cu(2+). Thus, the peroxide moiety receives electron equivalents from 
      cytochrome c without affecting the oxidation states of the metal sites. The 
      metal-site reduction is coupled to the proton pump.
FAU - Suga, Michihiro
AU  - Suga M
AD  - Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka 
      565-0871, Japan.
FAU - Yano, Naomine
AU  - Yano N
FAU - Muramoto, Kazumasa
AU  - Muramoto K
FAU - Shinzawa-Itoh, Kyoko
AU  - Shinzawa-Itoh K
FAU - Maeda, Tomoko
AU  - Maeda T
FAU - Yamashita, Eiki
AU  - Yamashita E
FAU - Tsukihara, Tomitake
AU  - Tsukihara T
FAU - Yoshikawa, Shinya
AU  - Yoshikawa S
LA  - eng
SI  - PDB/3ASN
SI  - PDB/3ASO
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110712
PL  - United States
TA  - Acta Crystallogr D Biol Crystallogr
JT  - Acta crystallographica. Section D, Biological crystallography
JID - 9305878
RN  - 4R7X1O2820 (Chlorine)
RN  - 789U1901C5 (Copper)
RN  - E1UOL152H7 (Iron)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Chlorine/*chemistry
MH  - Copper/*chemistry
MH  - Electron Transport Complex IV/*chemistry
MH  - Iron/*chemistry
MH  - Models, Molecular
MH  - Oxidation-Reduction
MH  - Oxygen/*chemistry
MH  - Protein Interaction Domains and Motifs
EDAT- 2011/07/29 06:00
MHDA- 2011/10/27 06:00
CRDT- 2011/07/29 06:00
PHST- 2011/04/07 00:00 [received]
PHST- 2011/06/13 00:00 [accepted]
PHST- 2011/07/29 06:00 [entrez]
PHST- 2011/07/29 06:00 [pubmed]
PHST- 2011/10/27 06:00 [medline]
AID - S0907444911022803 [pii]
AID - 10.1107/S0907444911022803 [doi]
PST - ppublish
SO  - Acta Crystallogr D Biol Crystallogr. 2011 Aug;67(Pt 8):742-4. doi: 
      10.1107/S0907444911022803. Epub 2011 Jul 12.