PMID- 27810193
OWN - NLM
STAT- MEDLINE
DCOM- 20171004
LR  - 20180917
IS  - 0005-2728 (Print)
IS  - 0005-2728 (Linking)
VI  - 1858
IP  - 2
DP  - 2017 Feb
TI  - Redox induced protonation of heme propionates in cytochrome c oxidase: Insights 
      from surface enhanced resonance Raman spectroscopy and QM/MM calculations.
PG  - 103-108
LID - S0005-2728(16)30652-1 [pii]
LID - 10.1016/j.bbabio.2016.10.009 [doi]
AB  - Understanding the coupling between heme reduction and proton translocation in 
      cytochrome c oxidase (CcO) is still an open problem. The propionic acids of heme 
      a(3) have been proposed to act as a proton loading site (PLS) in the proton 
      pumping pathway, yet this proposal could not be verified by experimental data so 
      far. We have set up an experiment where the redox states of the two hemes in CcO 
      can be controlled via external electrical potential. Surface enhanced resonance 
      Raman (SERR) spectroscopy was applied to simultaneously monitor the redox state 
      of the hemes and the protonation state of the heme propionates. Simulated spectra 
      based on QM/MM calculations were used to assign the resonant enhanced CH(2) 
      twisting modes of the propionates to the protonation state of the individual heme 
      a and heme a(3) propionates respectively. The comparison between calculated and 
      measured H(2)OD(2)O difference spectra allowed a sound band assignment. In the 
      fully reduced enzyme at least three of the four heme propionates were found to be 
      protonated whereas in the presence of a reduced heme a and an oxidized heme a(3) 
      only protonation of one heme a(3) propionates was observed. Our data supports the 
      postulated scenario where the heme a(3) propionates are involved in the proton 
      pathway.
CI  - Copyright (c) 2016 Elsevier B.V. All rights reserved.
FAU - Sezer, Murat
AU  - Sezer M
AD  - Institut fur Chemie PC 14, Technische Universitat Berlin, Strasse des 17. Juni 
      135, 10623 Berlin, Germany.
FAU - Woelke, Anna-Lena
AU  - Woelke AL
AD  - Institut fur Chemie und Biochemie, Freie Universitat Berlin, Fabeckstrasse 36a, 
      14195 Berlin, Germany.
FAU - Knapp, Ernst Walter
AU  - Knapp EW
AD  - Institut fur Chemie und Biochemie, Freie Universitat Berlin, Fabeckstrasse 36a, 
      14195 Berlin, Germany.
FAU - Schlesinger, Ramona
AU  - Schlesinger R
AD  - Institut fur Experimentalphysik, Freie Universitat Berlin, Arnimallee 14, 14195 
      Berlin, Germany.
FAU - Mroginski, Maria Andrea
AU  - Mroginski MA
AD  - Institut fur Chemie PC 14, Technische Universitat Berlin, Strasse des 17. Juni 
      135, 10623 Berlin, Germany.
FAU - Weidinger, Inez M
AU  - Weidinger IM
AD  - Institut fur Chemie PC 14, Technische Universitat Berlin, Strasse des 17. Juni 
      135, 10623 Berlin, Germany.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20161031
PL  - Netherlands
TA  - Biochim Biophys Acta Bioenerg
JT  - Biochimica et biophysica acta. Bioenergetics
JID - 101731706
RN  - 0 (Propionates)
RN  - 0 (Proton Pumps)
RN  - 0 (Protons)
RN  - 42VZT0U6YR (Heme)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Electron Transport Complex IV/*metabolism
MH  - Heme/*metabolism
MH  - Oxidation-Reduction
MH  - Propionates/*metabolism
MH  - Proton Pumps/metabolism
MH  - Protons
MH  - Spectrum Analysis, Raman/methods
OTO - NOTNLM
OT  - Cytochrome c oxidase
OT  - Proton loading site
OT  - Proton pumping
OT  - QM/MM calculations
OT  - Surface enhanced Raman spectroscopy
EDAT- 2016/11/05 06:00
MHDA- 2017/10/05 06:00
CRDT- 2016/11/05 06:00
PHST- 2016/07/22 00:00 [received]
PHST- 2016/10/18 00:00 [revised]
PHST- 2016/10/28 00:00 [accepted]
PHST- 2016/11/05 06:00 [pubmed]
PHST- 2017/10/05 06:00 [medline]
PHST- 2016/11/05 06:00 [entrez]
AID - S0005-2728(16)30652-1 [pii]
AID - 10.1016/j.bbabio.2016.10.009 [doi]
PST - ppublish
SO  - Biochim Biophys Acta Bioenerg. 2017 Feb;1858(2):103-108. doi: 
      10.1016/j.bbabio.2016.10.009. Epub 2016 Oct 31.