PMID- 20524628
OWN - NLM
STAT- MEDLINE
DCOM- 20100720
LR  - 20211020
IS  - 1520-4995 (Electronic)
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 49
IP  - 27
DP  - 2010 Jul 13
TI  - Mutagenic analysis of Cox11 of Rhodobacter sphaeroides: insights into the 
      assembly of Cu(B) of cytochrome c oxidase.
PG  - 5651-61
LID - 10.1021/bi1003876 [doi]
AB  - The Cu(I) chaperone Cox11 is required for the insertion of Cu(B) into cytochrome 
      c oxidase (CcO) of mitochondria and many bacteria, including Rhodobacter 
      sphaeroides. Exploration of the copper binding stoichiometry of R. sphaeroides 
      Cox11 led to the finding that an apparent tetramer of both mitochondrial and 
      bacterial Cox11 binds more copper than the sum of the dimers, providing another 
      example of the flexibility of copper binding by Cu(I)-S clusters. Site-directed 
      mutagenesis has been used to identify components of Cox11 that are not required 
      for copper binding but are absolutely required for the assembly of Cu(B), 
      including conserved Cys-35 and Lys-123. In contrast to earlier proposals, Cys-35 
      is not required for dimerization of Cox11 or for copper binding. These findings, 
      and the location of Cys-35 at the C-terminus of the predicted transmembrane helix 
      and thereby close to the surface of the membrane, allow a proposal that Cys-35 is 
      involved in the transfer of copper from the Cu(I) cluster of Cox11 to the Cu(B) 
      ligands His-333 and His-334 during the folding of CcO subunit I. Lys-123 is 
      located near the Cu(I) cluster of Cox11, in an area otherwise devoid of charged 
      residues. From the analysis of several Cox11 mutants, including K123E, -L, and 
      -R, we conclude that a previous proposal that Lys-123 provides charge balance for 
      the stabilization of the Cu(I) cluster is unlikely to account for its absolute 
      requirement for Cox11 function. Rather, consideration of the properties of 
      Lys-123 and the apparent specificity of Cox11 suggest that Lys-123 plays a role 
      in the interaction of Cox11 with its target.
FAU - Thompson, Audie K
AU  - Thompson AK
AD  - Department of Biochemistry, University of Mississippi Medical Center, Jackson, 
      Mississippi 39216, USA.
FAU - Smith, Daniel
AU  - Smith D
FAU - Gray, Jimmy
AU  - Gray J
FAU - Carr, Heather S
AU  - Carr HS
FAU - Liu, Aimin
AU  - Liu A
FAU - Winge, Dennis R
AU  - Winge DR
FAU - Hosler, Jonathan P
AU  - Hosler JP
LA  - eng
GR  - ES03817/ES/NIEHS NIH HHS/United States
GR  - GM56824/GM/NIGMS NIH HHS/United States
GR  - R01 GM056824/GM/NIGMS NIH HHS/United States
GR  - R01 ES003817/ES/NIEHS NIH HHS/United States
GR  - R37 ES003817/ES/NIEHS NIH HHS/United States
GR  - R01 GM056824-09/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Ligands)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Mutagens)
RN  - 789U1901C5 (Copper)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - K848JZ4886 (Cysteine)
SB  - IM
MH  - Copper/chemistry/*metabolism
MH  - Cysteine/genetics/metabolism
MH  - Dimerization
MH  - *Electron Transport Complex IV/chemistry/genetics/metabolism
MH  - Ligands
MH  - Molecular Chaperones/chemistry/genetics/metabolism
MH  - Mutagenesis, Site-Directed
MH  - Mutagens
MH  - Protein Structure, Secondary/genetics
MH  - Rhodobacter sphaeroides/*genetics/metabolism
PMC - PMC2994652
MID - NIHMS215874
EDAT- 2010/06/08 06:00
MHDA- 2010/07/21 06:00
PMCR- 2011/07/13
CRDT- 2010/06/08 06:00
PHST- 2010/06/08 06:00 [entrez]
PHST- 2010/06/08 06:00 [pubmed]
PHST- 2010/07/21 06:00 [medline]
PHST- 2011/07/13 00:00 [pmc-release]
AID - 10.1021/bi1003876 [doi]
PST - ppublish
SO  - Biochemistry. 2010 Jul 13;49(27):5651-61. doi: 10.1021/bi1003876.