PMID- 29435610
OWN - NLM
STAT- MEDLINE
DCOM- 20190909
LR  - 20190909
IS  - 1432-1424 (Electronic)
IS  - 0022-2631 (Linking)
VI  - 251
IP  - 3
DP  - 2018 Jun
TI  - Hydrogen-Bonded Network and Water Dynamics in the D-channel of Cytochrome c 
      Oxidase.
PG  - 299-314
LID - 10.1007/s00232-018-0019-x [doi]
AB  - Proton transfer in cytochrome c oxidase (CcO) from the cellular inside to the 
      binuclear redox centre as well as proton pumping through the membrane takes place 
      through proton entrance via two distinct pathways, the D- and K-channel. Both 
      channels show a dependence of their hydration level on the protonation states of 
      their key residues, K362 for the K-channel, and E286 or D132 for the D-channel. 
      In the oxidative half of CcO's catalytic cycle the D-channel is the 
      proton-conducting path. For this channel, an interplay of protonation state of 
      the D-channel residues with the water and hydrogen-bond dynamics has been 
      observed in molecular dynamics simulations of the CcO protein, embedded in a 
      lipid bi-layer, modelled in different protonation states. Protonation of residue 
      E286 at the end of the D-channel results in a hydrogen-bonded network pointing 
      from E286 to N139, that is against proton transport, and favouring N139 
      conformations which correspond to a closed asparagine gate (formed by residues 
      N121 and N139). Consequently, the hydration level is lower than with unprotonated 
      E286. In those models, the Asn gate is predominantly open, allowing water 
      molecules to pass and thus increase the hydration level. The hydrogen-bonded 
      network in these states exhibits longer life times of the Asn residues with water 
      than other models and shows the D-channel to be traversable from the entrance, 
      D132, to exit, E286. The D-channel can thus be regarded as auto-regulated with 
      respect to proton transport, allowing proton passage only when required, that is 
      the proton is located at the lower part of the D-channel (D132 to Asn gate) and 
      not at the exit (E286).
FAU - Ghane, Tahereh
AU  - Ghane T
AD  - Institute of Theoretical Physics, Freie Universitat Berlin, Arnimallee 14, 14195, 
      Berlin, Germany.
FAU - Gorriz, Rene F
AU  - Gorriz RF
AD  - Institute of Theoretical Physics, Freie Universitat Berlin, Arnimallee 14, 14195, 
      Berlin, Germany.
FAU - Wrzalek, Sandro
AU  - Wrzalek S
AD  - Institute of Theoretical Physics, Freie Universitat Berlin, Arnimallee 14, 14195, 
      Berlin, Germany.
FAU - Volkenandt, Senta
AU  - Volkenandt S
AD  - Institute of Theoretical Physics, Freie Universitat Berlin, Arnimallee 14, 14195, 
      Berlin, Germany.
FAU - Dalatieh, Ferand
AU  - Dalatieh F
AD  - Institute of Theoretical Physics, Freie Universitat Berlin, Arnimallee 14, 14195, 
      Berlin, Germany.
AD  - R Institute GmbH, Dortustrasse 48, 14467, Potsdam, Germany.
FAU - Reidelbach, Marco
AU  - Reidelbach M
AD  - Institute of Theoretical Physics, Freie Universitat Berlin, Arnimallee 14, 14195, 
      Berlin, Germany.
FAU - Imhof, Petra
AU  - Imhof P
AUID- ORCID: 0000-0001-9820-4578
AD  - Institute of Theoretical Physics, Freie Universitat Berlin, Arnimallee 14, 14195, 
      Berlin, Germany. petra.imhof@fu-berlin.de.
LA  - eng
GR  - C5 in SFB1078/Deutsche Forschungsgemeinschaft/International
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20180212
PL  - United States
TA  - J Membr Biol
JT  - The Journal of membrane biology
JID - 0211301
RN  - 0 (Membrane Proteins)
RN  - 0 (Protons)
RN  - 059QF0KO0R (Water)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Electron Transport Complex IV/chemistry/*metabolism
MH  - Hydrogen Bonding
MH  - Membrane Proteins/chemistry/metabolism
MH  - Molecular Dynamics Simulation
MH  - Protein Conformation
MH  - Protons
MH  - Water/*metabolism
OTO - NOTNLM
OT  - Cytochrome c oxidase
OT  - Membrane protein
OT  - Proton transfer
EDAT- 2018/02/13 06:00
MHDA- 2019/09/10 06:00
CRDT- 2018/02/14 06:00
PHST- 2017/10/24 00:00 [received]
PHST- 2018/02/06 00:00 [accepted]
PHST- 2018/02/13 06:00 [pubmed]
PHST- 2019/09/10 06:00 [medline]
PHST- 2018/02/14 06:00 [entrez]
AID - 10.1007/s00232-018-0019-x [pii]
AID - 10.1007/s00232-018-0019-x [doi]
PST - ppublish
SO  - J Membr Biol. 2018 Jun;251(3):299-314. doi: 10.1007/s00232-018-0019-x. Epub 2018 
      Feb 12.