PMID- 11557043
OWN - NLM
STAT- MEDLINE
DCOM- 20011025
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 505
IP  - 1
DP  - 2001 Sep 7
TI  - Perfusion-induced redox differences in cytochrome c oxidase: ATR/FT-IR 
      spectroscopy.
PG  - 63-7
AB  - Attenuated total reflection (ATR) spectroscopy brings an added dimension to 
      studies of structural changes of cytochrome c oxidase (CcO) because it enables 
      the recording of reaction-induced infrared difference spectra under a wide 
      variety of controlled conditions (e.g. pH and chemical composition), without 
      relying on light or potentiometric changes to trigger the reaction. We have used 
      the ATR method to record vibrational difference spectra of CcO with reduction 
      induced by flow-exchange of the aqueous buffer. Films of CcO prepared from 
      Rhodobacter sphaeroides and beef heart mitochondria by reconstitution with lipid 
      were adhered to the internal reflection element of the ATR device and retained 
      their full functionality as evidenced by visible spectroscopy and time-resolved 
      vibrational spectroscopy. These results demonstrate that the technique of 
      perfusion-induced Fourier-transform infrared difference spectroscopy can be 
      successfully applied to a large, complex enzyme, such as CcO, with sufficient 
      signal/noise to probe vibrational changes in individual residues of the enzyme 
      under various conditions.
FAU - Nyquist, R M
AU  - Nyquist RM
AD  - Forschungszentrum Julich, IBI-2: Biologische Strukturforschung, Germany.
FAU - Heitbrink, D
AU  - Heitbrink D
FAU - Bolwien, C
AU  - Bolwien C
FAU - Wells, T A
AU  - Wells TA
FAU - Gennis, R B
AU  - Gennis RB
FAU - Heberle, J
AU  - Heberle J
LA  - eng
GR  - 5-T32 GMO8276-13/GM/NIGMS NIH HHS/United States
GR  - HL16101/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Enzymes, Immobilized)
RN  - 0 (Phospholipids)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Animals
MH  - Cattle
MH  - Electron Transport Complex IV/*chemistry/*metabolism
MH  - Enzymes, Immobilized/chemistry/metabolism
MH  - Mitochondria, Heart/enzymology
MH  - Oxidation-Reduction
MH  - Perfusion
MH  - Phospholipids/chemistry
MH  - Rhodobacter sphaeroides/enzymology
MH  - Spectroscopy, Fourier Transform Infrared/*methods
MH  - Vibration
EDAT- 2001/09/15 10:00
MHDA- 2001/10/26 10:01
CRDT- 2001/09/15 10:00
PHST- 2001/09/15 10:00 [pubmed]
PHST- 2001/10/26 10:01 [medline]
PHST- 2001/09/15 10:00 [entrez]
AID - S0014-5793(01)02769-7 [pii]
AID - 10.1016/s0014-5793(01)02769-7 [doi]
PST - ppublish
SO  - FEBS Lett. 2001 Sep 7;505(1):63-7. doi: 10.1016/s0014-5793(01)02769-7.