PMID- 21541411
OWN - NLM
STAT- MEDLINE
DCOM- 20111004
LR  - 20211020
IS  - 1756-591X (Electronic)
IS  - 1756-5901 (Print)
IS  - 1756-5901 (Linking)
VI  - 3
IP  - 6
DP  - 2011 Jun
TI  - 2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c 
      oxidase induced by direct electron transfer.
PG  - 619-27
LID - 10.1039/c0mt00083c [doi]
AB  - Potentiometric titrations of the cytochrome c oxidase (CcO) immobilized in a 
      biomimetic membrane system were followed by two-dimensional surface-enhanced IR 
      absorption spectroscopy (2D SEIRAS) in the ATR-mode. Direct electron transfer was 
      employed to vary the redox state of the enzyme. The CcO was shown to undergo a 
      conformational transition from a non-activated to an activated state after it was 
      allowed to turnover in the presence of oxygen. Differences between the 
      non-activated and activated state were revealed by 2D SEIRA spectra recorded as a 
      function of potential. The activated state was characterized by a higher number 
      of correlated transitions as well as a higher number of amino acids associated 
      with electron transfer.
FAU - Nowak, Christoph
AU  - Nowak C
AD  - Austrian Institute of Technology GmbH, AIT, Donau-City Str. 1, 1220 Vienna, 
      Austria. C.Nowak@ait.ac.at
FAU - Laredo, Thamara
AU  - Laredo T
FAU - Gebert, Jens
AU  - Gebert J
FAU - Lipkowski, Jacek
AU  - Lipkowski J
FAU - Gennis, Robert B
AU  - Gennis RB
FAU - Ferguson-Miller, Shelagh
AU  - Ferguson-Miller S
FAU - Knoll, Wolfgang
AU  - Knoll W
FAU - Naumann, Renate L C
AU  - Naumann RL
LA  - eng
GR  - R01 GM026916/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110504
PL  - England
TA  - Metallomics
JT  - Metallomics : integrated biometal science
JID - 101478346
RN  - 0 (Amino Acids)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Protein Subunits)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Amino Acids/chemistry/metabolism
MH  - Bacterial Proteins/*chemistry/metabolism
MH  - Crystallography, X-Ray
MH  - Electrochemical Techniques/*methods
MH  - Electron Transport
MH  - Electron Transport Complex IV/*chemistry/metabolism
MH  - Enzyme Activation
MH  - Hydrophobic and Hydrophilic Interactions
MH  - Models, Molecular
MH  - Oxidation-Reduction
MH  - Oxygen/chemistry/metabolism
MH  - *Protein Conformation
MH  - Protein Subunits/chemistry/metabolism
MH  - Rhodobacter sphaeroides/enzymology
MH  - Spectroscopy, Fourier Transform Infrared/*methods
PMC - PMC3912184
MID - NIHMS547713
EDAT- 2011/05/05 06:00
MHDA- 2011/10/05 06:00
PMCR- 2014/02/03
CRDT- 2011/05/05 06:00
PHST- 2011/05/05 06:00 [entrez]
PHST- 2011/05/05 06:00 [pubmed]
PHST- 2011/10/05 06:00 [medline]
PHST- 2014/02/03 00:00 [pmc-release]
AID - 10.1039/c0mt00083c [doi]
PST - ppublish
SO  - Metallomics. 2011 Jun;3(6):619-27. doi: 10.1039/c0mt00083c. Epub 2011 May 4.