PMID- 17239857
OWN - NLM
STAT- MEDLINE
DCOM- 20070312
LR  - 20181113
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 581
IP  - 3
DP  - 2007 Feb 6
TI  - Tryptophan 334 oxidation in bovine cytochrome c oxidase subunit I involves free 
      radical migration.
PG  - 437-42
AB  - A single tryptophan (W(334(I))) within the mitochondrial-encoded core subunits of 
      cytochrome c oxidase (CcO) is selectively oxidized when hydrogen peroxide reacts 
      with the binuclear center. W(334(I)) is converted to hydroxytryptophan as 
      identified by reversed-phase HPLC-electrospray ionization tandem mass 
      spectrometry analysis of peptides derived from the three SDS-PAGE purified 
      subunits. Total sequence coverage of subunits I, II and III was limited to 84%, 
      66% and 54%, respectively. W(334(I)) is located on the surface of CcO at the 
      membrane interface. Two other surface tryptophans within nuclear-encoded 
      subunits, W(48(IV)) and W(19(VIIc)), are also oxidized when hydrogen peroxide 
      reacts with the binuclear center (Musatov et al. (2004) Biochemistry 43, 
      1003-1009). Two aromatic-rich networks of amino acids were identified that link 
      the binuclear center to the three oxidized tryptophans. We propose the following 
      mechanism to explain these results. Electron transfer through the aromatic 
      networks moves the free radicals generated at the binuclear center to the 
      surface-exposed tryptophans, where they produce hydroxytryptophan.
FAU - Lemma-Gray, Patrizia
AU  - Lemma-Gray P
AD  - Department of Biochemistry, The University of Texas Health Science Center, MC 
      7760, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA.
FAU - Weintraub, Susan T
AU  - Weintraub ST
FAU - Carroll, Christopher A
AU  - Carroll CA
FAU - Musatov, Andrej
AU  - Musatov A
FAU - Robinson, Neal C
AU  - Robinson NC
LA  - eng
GR  - P30 AG013319/AG/NIA NIH HHS/United States
GR  - R01 GM024795/GM/NIGMS NIH HHS/United States
GR  - AG013319-11/AG/NIA NIH HHS/United States
GR  - GM24795/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20070112
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Free Radicals)
RN  - 0 (Peptide Fragments)
RN  - 0 (Protein Subunits)
RN  - 8DUH1N11BX (Tryptophan)
RN  - BBX060AN9V (Hydrogen Peroxide)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Cattle
MH  - Chromatography, High Pressure Liquid
MH  - Electron Transport
MH  - Electron Transport Complex IV/*chemistry/genetics/metabolism
MH  - Free Radicals/chemistry
MH  - Hydrogen Peroxide/metabolism
MH  - In Vitro Techniques
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Oxidation-Reduction
MH  - Peptide Fragments/chemistry/genetics/metabolism
MH  - Protein Subunits
MH  - Spectrometry, Mass, Electrospray Ionization
MH  - Tryptophan/chemistry
PMC - PMC1931429
MID - NIHMS17634
EDAT- 2007/01/24 09:00
MHDA- 2007/03/14 09:00
PMCR- 2008/02/06
CRDT- 2007/01/24 09:00
PHST- 2006/12/21 00:00 [received]
PHST- 2006/12/25 00:00 [accepted]
PHST- 2007/01/24 09:00 [pubmed]
PHST- 2007/03/14 09:00 [medline]
PHST- 2007/01/24 09:00 [entrez]
PHST- 2008/02/06 00:00 [pmc-release]
AID - S0014-5793(07)00023-3 [pii]
AID - 10.1016/j.febslet.2006.12.054 [doi]
PST - ppublish
SO  - FEBS Lett. 2007 Feb 6;581(3):437-42. doi: 10.1016/j.febslet.2006.12.054. Epub 
      2007 Jan 12.