PMID- 32250438
OWN - NLM
STAT- MEDLINE
DCOM- 20201204
LR  - 20201214
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 477
IP  - 8
DP  - 2020 Apr 30
TI  - Osmotic pressure effects identify dehydration upon cytochrome c-cytochrome c 
      oxidase complex formation contributing to a specific electron pathway formation.
PG  - 1565-1578
LID - 10.1042/BCJ20200023 [doi]
AB  - In the electron transfer (ET) reaction from cytochrome c (Cyt c) to cytochrome c 
      oxidase (CcO), we determined the number and sites of the hydration water released 
      from the protein surface upon the formation of the ET complex by evaluating the 
      osmotic pressure dependence of kinetics for the ET from Cyt c to CcO. We 
      identified that  approximately 20 water molecules were dehydrated in complex formation under 
      turnover conditions, and systematic Cyt c mutations in the interaction site for 
      CcO revealed that nearly half of the released hydration water during the 
      complexation were located around Ile81, one of the hydrophobic amino acid 
      residues near the exposed heme periphery of Cyt c. Such a dehydration dominantly 
      compensates for the entropy decrease due to the association of Cyt c with CcO, 
      resulting in the entropy-driven ET reaction. The energetic analysis of the 
      interprotein interactions in the ET complex predicted by the docking simulation 
      suggested the formation of hydrophobic interaction sites surrounding the exposed 
      heme periphery of Cyt c in the Cyt c-CcO interface (a 'molecular breakwater'). 
      Such sites would contribute to the formation of the hydrophobic ET pathway from 
      Cyt c to CcO by blocking water access from the bulk water phase.
CI  - (c) 2020 The Author(s). Published by Portland Press Limited on behalf of the 
      Biochemical Society.
FAU - Sato, Wataru
AU  - Sato W
AD  - Graduate School of Chemical Sciences and Engineering, Hokkaido University, 
      Sapporo 060-8628, Japan.
FAU - Hitaoka, Seiji
AU  - Hitaoka S
AD  - Institute for Materials Chemistry and Engineering, Kyushu University, Fukuoka 
      819-0315, Japan.
FAU - Uchida, Takeshi
AU  - Uchida T
AD  - Graduate School of Chemical Sciences and Engineering, Hokkaido University, 
      Sapporo 060-8628, Japan.
AD  - Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 
      060-0810, Japan.
FAU - Shinzawa-Itoh, Kyoko
AU  - Shinzawa-Itoh K
AD  - Picobiology Institute, Graduate School of Life Science, University of Hyogo, 
      Ako-gun, Hyogo 678-1297, Japan.
FAU - Yoshizawa, Kazunari
AU  - Yoshizawa K
AD  - Institute for Materials Chemistry and Engineering, Kyushu University, Fukuoka 
      819-0315, Japan.
FAU - Yoshikawa, Shinya
AU  - Yoshikawa S
AD  - Picobiology Institute, Graduate School of Life Science, University of Hyogo, 
      Ako-gun, Hyogo 678-1297, Japan.
FAU - Ishimori, Koichiro
AU  - Ishimori K
AD  - Graduate School of Chemical Sciences and Engineering, Hokkaido University, 
      Sapporo 060-8628, Japan.
AD  - Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo 
      060-0810, Japan.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Escherichia coli Proteins)
RN  - 059QF0KO0R (Water)
RN  - 9007-43-6 (Cytochromes c)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
SB  - IM
MH  - Cytochromes c/*chemistry/metabolism
MH  - Electron Transport
MH  - Electron Transport Complex IV/*chemistry/metabolism
MH  - Entropy
MH  - Escherichia coli/chemistry/*metabolism
MH  - Escherichia coli Proteins/chemistry/*metabolism
MH  - Humans
MH  - Hydrophobic and Hydrophilic Interactions
MH  - Kinetics
MH  - Models, Molecular
MH  - Molecular Docking Simulation
MH  - Osmotic Pressure
MH  - Oxidation-Reduction
MH  - Water/*chemistry/metabolism
OTO - NOTNLM
OT  - complex IV
OT  - cytochrome c
OT  - dehydration
OT  - electron transfer
OT  - osmotic pressure
EDAT- 2020/04/07 06:00
MHDA- 2020/12/15 06:00
CRDT- 2020/04/07 06:00
PHST- 2020/01/21 00:00 [received]
PHST- 2020/03/27 00:00 [revised]
PHST- 2020/04/06 00:00 [accepted]
PHST- 2020/04/07 06:00 [pubmed]
PHST- 2020/12/15 06:00 [medline]
PHST- 2020/04/07 06:00 [entrez]
AID - 222579 [pii]
AID - 10.1042/BCJ20200023 [doi]
PST - ppublish
SO  - Biochem J. 2020 Apr 30;477(8):1565-1578. doi: 10.1042/BCJ20200023.