PMID- 23996000
OWN - NLM
STAT- MEDLINE
DCOM- 20131231
LR  - 20211021
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 288
IP  - 42
DP  - 2013 Oct 18
TI  - Effective pumping proton collection facilitated by a copper site (CuB) of bovine 
      heart cytochrome c oxidase, revealed by a newly developed time-resolved infrared 
      system.
PG  - 30259-30269
LID - S0021-9258(20)85700-7 [pii]
LID - 10.1074/jbc.M113.473983 [doi]
AB  - X-ray structural and mutational analyses have shown that bovine heart cytochrome 
      c oxidase (CcO) pumps protons electrostatically through a hydrogen bond network 
      using net positive charges created upon oxidation of a heme iron (located near 
      the hydrogen bond network) for O2 reduction. Pumping protons are transferred by 
      mobile water molecules from the negative side of the mitochondrial inner membrane 
      through a water channel into the hydrogen bond network. For blockage of 
      spontaneous proton back-leak, the water channel is closed upon O2 binding to the 
      second heme (heme a3) after complete collection of the pumping protons in the 
      hydrogen bond network. For elucidation of the structural bases for the mechanism 
      of the proton collection and timely closure of the water channel, conformational 
      dynamics after photolysis of CO (an O2 analog)-bound CcO was examined using a 
      newly developed time-resolved infrared system feasible for accurate detection of 
      a single C=O stretch band of alpha-helices of CcO in H2O medium. The present results 
      indicate that migration of CO from heme a3 to CuB in the O2 reduction site 
      induces an intermediate state in which a bulge conformation at Ser-382 in a 
      transmembrane helix is eliminated to open the water channel. The structural 
      changes suggest that, using a conformational relay system, including CuB, O2, 
      heme a3, and two helix turns extending to Ser-382, CuB induces the conformational 
      changes of the water channel that stimulate the proton collection, and senses 
      complete proton loading into the hydrogen bond network to trigger the timely 
      channel closure by O2 transfer from CuB to heme a3.
FAU - Kubo, Minoru
AU  - Kubo M
AD  - From the Picobiology Institute,; PRESTO and.
FAU - Nakashima, Satoru
AU  - Nakashima S
AD  - From the Picobiology Institute.
FAU - Yamaguchi, Satoru
AU  - Yamaguchi S
AD  - Department of Life Science, Graduate School of Life Science, University of Hyogo, 
      3-2-1 Kouto, Kamighori, Akoh, Hyogo 678-1297 and.
FAU - Ogura, Takashi
AU  - Ogura T
AD  - From the Picobiology Institute,; Department of Life Science, Graduate School of 
      Life Science, University of Hyogo, 3-2-1 Kouto, Kamighori, Akoh, Hyogo 678-1297 
      and; CREST, Japan Science and Technology Agency, 4-1-8 Honcho, Kawaguchi, Saitama 
      332-0012, Japan.
FAU - Mochizuki, Masao
AU  - Mochizuki M
AD  - From the Picobiology Institute.
FAU - Kang, Jiyoung
AU  - Kang J
AD  - From the Picobiology Institute.
FAU - Tateno, Masaru
AU  - Tateno M
AD  - From the Picobiology Institute,; CREST, Japan Science and Technology Agency, 
      4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan.
FAU - Shinzawa-Itoh, Kyoko
AU  - Shinzawa-Itoh K
AD  - From the Picobiology Institute.
FAU - Kato, Koji
AU  - Kato K
AD  - From the Picobiology Institute.
FAU - Yoshikawa, Shinya
AU  - Yoshikawa S
AD  - From the Picobiology Institute,; CREST, Japan Science and Technology Agency, 
      4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan. Electronic address: 
      yoshi@sci.u-hyogo.ac.jp.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130830
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Muscle Proteins)
RN  - 0 (Proton Pumps)
RN  - 42VZT0U6YR (Heme)
RN  - 789U1901C5 (Copper)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Cattle
MH  - Copper/*chemistry/metabolism
MH  - Electron Transport Complex IV/*chemistry/metabolism
MH  - Heme/chemistry/metabolism
MH  - Muscle Proteins/*chemistry/metabolism
MH  - Myocardium/*enzymology
MH  - Protein Structure, Secondary
MH  - Proton Pumps/chemistry/metabolism
MH  - Spectrophotometry, Infrared
PMC - PMC3798492
OTO - NOTNLM
OT  - Bioenergetics
OT  - Biophysics
OT  - Infrared Spectroscopy
OT  - Membrane Proteins
OT  - Respiratory Chain
EDAT- 2013/09/03 06:00
MHDA- 2014/01/01 06:00
PMCR- 2014/10/18
CRDT- 2013/09/03 06:00
PHST- 2013/09/03 06:00 [entrez]
PHST- 2013/09/03 06:00 [pubmed]
PHST- 2014/01/01 06:00 [medline]
PHST- 2014/10/18 00:00 [pmc-release]
AID - S0021-9258(20)85700-7 [pii]
AID - M113.473983 [pii]
AID - 10.1074/jbc.M113.473983 [doi]
PST - ppublish
SO  - J Biol Chem. 2013 Oct 18;288(42):30259-30269. doi: 10.1074/jbc.M113.473983. Epub 
      2013 Aug 30.