PMID- 15963451
OWN - NLM
STAT- MEDLINE
DCOM- 20050901
LR  - 20161019
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 439
IP  - 2
DP  - 2005 Jul 15
TI  - Involvement of phospholipid, biomembrane integrity, and NO peroxidase activity in 
      the NO catabolism by cytochrome c oxidase.
PG  - 200-10
AB  - The physiological regulation of mitochondrial respiration by NO has been reported 
      to result from the reversible binding of NO to the two-electron reduced binuclear 
      center (Fe(2+)(a3)-Cu(1+)(B)) of cytochrome c oxidase (CcO). Although the role of 
      CcO and its derived catalytic intermediates in the catabolism of NO has been 
      documented, little has been established for the enzyme in its fully oxidized 
      state (Fe(3+)(a3)-Cu(2+)(B)). We report: (1) CcO, in its fully oxidized state, 
      represents the major component of the mitochondrial electron transport chain for 
      NO consumption as controlled by the binding of NO to its binuclear center. 
      Phospholipid enhances NO consumption by fully oxidized CcO, whereas the 
      consumption of NO is slowed down by membrane structure and membrane potential 
      when CcO is embedded in the phospholipid bilayer. (2) In the presence of 
      H(2)O(2), CcO was shown to serve as a mitochondria-derived NO peroxidase. A 
      CcO-derived protein radical intermediate was induced and involved in the 
      modulation of NO catabolism.
FAU - Chen, Yeong-Renn
AU  - Chen YR
AD  - Davis Heart and Lung Research Institute, Division of Cardiovascular Medicine, 
      Department of Internal Medicine, The Ohio State University, College of Medicine, 
      Columbus, 43210, USA. chen-12@medctr.osu.edu
FAU - Chen, Chwen-Lih
AU  - Chen CL
FAU - Liu, Xiaoping
AU  - Liu X
FAU - He, Guanglong
AU  - He G
FAU - Zweier, Jay L
AU  - Zweier JL
LA  - eng
GR  - K22-ES11031/ES/NIEHS NIH HHS/United States
GR  - HL63744/HL/NHLBI NIH HHS/United States
GR  - K22 ES011031/ES/NIEHS NIH HHS/United States
GR  - HL65608/HL/NHLBI NIH HHS/United States
GR  - R01 HL38324/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Free Radicals)
RN  - 0 (Phospholipids)
RN  - 31C4KY9ESH (Nitric Oxide)
RN  - 42HK56048U (Tyrosine)
RN  - BBX060AN9V (Hydrogen Peroxide)
RN  - EC 1.11.1.7 (Peroxidase)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Animals
MH  - Cattle
MH  - Electron Transport Complex IV/drug effects/*metabolism
MH  - Free Radicals/metabolism
MH  - Hydrogen Peroxide/metabolism/pharmacology
MH  - Intracellular Membranes/chemistry/*metabolism
MH  - Mitochondria/chemistry/metabolism
MH  - Nitric Oxide/*metabolism
MH  - Oxidation-Reduction
MH  - Peroxidase/*metabolism
MH  - Phospholipids/*metabolism
MH  - Polarography
MH  - Spectrophotometry, Ultraviolet
MH  - Submitochondrial Particles/chemistry/metabolism
MH  - Tyrosine/metabolism
EDAT- 2005/06/21 09:00
MHDA- 2005/09/02 09:00
CRDT- 2005/06/21 09:00
PHST- 2005/04/13 00:00 [received]
PHST- 2005/05/09 00:00 [revised]
PHST- 2005/05/10 00:00 [accepted]
PHST- 2005/06/21 09:00 [pubmed]
PHST- 2005/09/02 09:00 [medline]
PHST- 2005/06/21 09:00 [entrez]
AID - S0003-9861(05)00207-9 [pii]
AID - 10.1016/j.abb.2005.05.014 [doi]
PST - ppublish
SO  - Arch Biochem Biophys. 2005 Jul 15;439(2):200-10. doi: 10.1016/j.abb.2005.05.014.