The interaction of coenzyme Q with phosphatidylethanolamine membranes

Coenzyme Q (CoQ) is a component of the mitochondrial respiratory chain which carries out additional membrane functions, such as acting as an antioxidant. The location of CoQ in the membrane and the interaction with the phospholipid bilayer is still a subject of debate. The interaction of CoQ in the...

Full description

Saved in:
Bibliographic Details
Published inEuropean journal of biochemistry Vol. 259; no. 3; pp. 739 - 746
Main Authors Gómez‐Fernández, Juan C., Llamas, Maria A., Aranda, Francisco J.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Science Ltd 01.02.1999
Subjects
Online AccessGet full text
ISSN0014-2956
1432-1033
DOI10.1046/j.1432-1327.1999.00109.x

Cover

Loading…
Abstract Coenzyme Q (CoQ) is a component of the mitochondrial respiratory chain which carries out additional membrane functions, such as acting as an antioxidant. The location of CoQ in the membrane and the interaction with the phospholipid bilayer is still a subject of debate. The interaction of CoQ in the oxidized (ubiquinone‐10) and reduced (ubiquinol‐10) state with membrane model systems of 1,2‐dielaidoyl‐sn‐glycero‐3‐phosphoethanolamine (Ela2Gro‐P‐Etn) has been studied by means of differential scanning calorimetry (DSC), 31P‐nuclear magnetic resonance (31P‐NMR) and small angle X‐ray diffraction (SAXD). Ubiquinone‐10 did not visibly affect the lamellar gel to lamellar liquid‐crystalline phase transition of Ela2Gro‐P‐Etn, but it clearly perturbed the multicomponent lamellar liquid‐crystalline to lamellar gel phase transition of the phospholipid. The perturbation of both transitions was more effective in the presence of ubiquinol‐10. A location of CoQ forming head to head aggregates in the center of the Ela2Gro‐P‐Etn bilayer with the polar rings protruding toward the phospholipid acyl chains is suggested. The formation of such aggregates are compatible with the strong hexagonal HII phase promotion ability found for CoQ. This ability was evidenced by the shifting of the lamellar to hexagonal HII phase transition to lower temperatures and by the appearance of the characteristic hexagonal HII31P‐NMR resonance and SAXD pattern at temperatures at which the pure Ela2Gro‐P‐Etn is still organized in extended bilayer structures. The influence of CoQ on the thermotropic properties and phase behavior of Ela2Gro‐P‐Etn is discussed in relation to the role of CoQ in the membrane.
AbstractList Coenzyme Q (CoQ) is a component of the mitochondrial respiratory chain which carries out additional membrane functions, such as acting as an antioxidant. The location of CoQ in the membrane and the interaction with the phospholipid bilayer is still a subject of debate. The interaction of CoQ in the oxidized (ubiquinone‐10) and reduced (ubiquinol‐10) state with membrane model systems of 1,2‐dielaidoyl‐ sn ‐glycero‐3‐phosphoethanolamine (Ela 2 Gro‐P‐Etn) has been studied by means of differential scanning calorimetry (DSC), 31 P‐nuclear magnetic resonance ( 31 P‐NMR) and small angle X‐ray diffraction (SAXD). Ubiquinone‐10 did not visibly affect the lamellar gel to lamellar liquid‐crystalline phase transition of Ela 2 Gro‐P‐Etn, but it clearly perturbed the multicomponent lamellar liquid‐crystalline to lamellar gel phase transition of the phospholipid. The perturbation of both transitions was more effective in the presence of ubiquinol‐10. A location of CoQ forming head to head aggregates in the center of the Ela 2 Gro‐P‐Etn bilayer with the polar rings protruding toward the phospholipid acyl chains is suggested. The formation of such aggregates are compatible with the strong hexagonal H II phase promotion ability found for CoQ. This ability was evidenced by the shifting of the lamellar to hexagonal H II phase transition to lower temperatures and by the appearance of the characteristic hexagonal H II 31 P‐NMR resonance and SAXD pattern at temperatures at which the pure Ela 2 Gro‐P‐Etn is still organized in extended bilayer structures. The influence of CoQ on the thermotropic properties and phase behavior of Ela 2 Gro‐P‐Etn is discussed in relation to the role of CoQ in the membrane.
Coenzyme Q (CoQ) is a component of the mitochondrial respiratory chain which carries out additional membrane functions, such as acting as an antioxidant. The location of CoQ in the membrane and the interaction with the phospholipid bilayer is still a subject of debate. The interaction of CoQ in the oxidized (ubiquinone‐10) and reduced (ubiquinol‐10) state with membrane model systems of 1,2‐dielaidoyl‐sn‐glycero‐3‐phosphoethanolamine (Ela2Gro‐P‐Etn) has been studied by means of differential scanning calorimetry (DSC), 31P‐nuclear magnetic resonance (31P‐NMR) and small angle X‐ray diffraction (SAXD). Ubiquinone‐10 did not visibly affect the lamellar gel to lamellar liquid‐crystalline phase transition of Ela2Gro‐P‐Etn, but it clearly perturbed the multicomponent lamellar liquid‐crystalline to lamellar gel phase transition of the phospholipid. The perturbation of both transitions was more effective in the presence of ubiquinol‐10. A location of CoQ forming head to head aggregates in the center of the Ela2Gro‐P‐Etn bilayer with the polar rings protruding toward the phospholipid acyl chains is suggested. The formation of such aggregates are compatible with the strong hexagonal HII phase promotion ability found for CoQ. This ability was evidenced by the shifting of the lamellar to hexagonal HII phase transition to lower temperatures and by the appearance of the characteristic hexagonal HII31P‐NMR resonance and SAXD pattern at temperatures at which the pure Ela2Gro‐P‐Etn is still organized in extended bilayer structures. The influence of CoQ on the thermotropic properties and phase behavior of Ela2Gro‐P‐Etn is discussed in relation to the role of CoQ in the membrane.
Coenzyme Q (CoQ) is a component of the mitochondrial respiratory chain which carries out additional membrane functions, such as acting as an antioxidant. The location of CoQ in the membrane and the interaction with the phospholipid bilayer is still a subject of debate. The interaction of CoQ in the oxidized (ubiquinone-10) and reduced (ubiquinol-10) state with membrane model systems of 1,2-dielaidoyl-sn-glycero-3-phosphoethanolamine (Ela2Gro-P-Etn) has been studied by means of differential scanning calorimetry (DSC), 31P-nuclear magnetic resonance (31P-NMR) and small angle X-ray diffraction (SAXD). Ubiquinone-10 did not visibly affect the lamellar gel to lamellar liquid-crystalline phase transition of Ela2Gro-P-Etn, but it clearly perturbed the multicomponent lamellar liquid-crystalline to lamellar gel phase transition of the phospholipid. The perturbation of both transitions was more effective in the presence of ubiquinol-10. A location of CoQ forming head to head aggregates in the center of the Ela2Gro-P-Etn bilayer with the polar rings protruding toward the phospholipid acyl chains is suggested. The formation of such aggregates are compatible with the strong hexagonal HII phase promotion ability found for CoQ. This ability was evidenced by the shifting of the lamellar to hexagonal HII phase transition to lower temperatures and by the appearance of the characteristic hexagonal HII 31P-NMR resonance and SAXD pattern at temperatures at which the pure Ela2Gro-P-Etn is still organized in extended bilayer structures. The influence of CoQ on the thermotropic properties and phase behavior of Ela2Gro-P-Etn is discussed in relation to the role of CoQ in the membrane.
Coenzyme Q (CoQ) is a component of the mitochondrial respiratory chain which carries out additional membrane functions, such as acting as an antioxidant. The location of CoQ in the membrane and the interaction with the phospholipid bilayer is still a subject of debate. The interaction of CoQ in the oxidized (ubiquinone-10) and reduced (ubiquinol-10) state with membrane model systems of 1,2-dielaidoyl-sn-glycero-3-phosphoethanolamine (Ela2Gro-P-Etn) has been studied by means of differential scanning calorimetry (DSC), 31P-nuclear magnetic resonance (31P-NMR) and small angle X-ray diffraction (SAXD). Ubiquinone-10 did not visibly affect the lamellar gel to lamellar liquid-crystalline phase transition of Ela2Gro-P-Etn, but it clearly perturbed the multicomponent lamellar liquid-crystalline to lamellar gel phase transition of the phospholipid. The perturbation of both transitions was more effective in the presence of ubiquinol-10. A location of CoQ forming head to head aggregates in the center of the Ela2Gro-P-Etn bilayer with the polar rings protruding toward the phospholipid acyl chains is suggested. The formation of such aggregates are compatible with the strong hexagonal HII phase promotion ability found for CoQ. This ability was evidenced by the shifting of the lamellar to hexagonal HII phase transition to lower temperatures and by the appearance of the characteristic hexagonal HII 31P-NMR resonance and SAXD pattern at temperatures at which the pure Ela2Gro-P-Etn is still organized in extended bilayer structures. The influence of CoQ on the thermotropic properties and phase behavior of Ela2Gro-P-Etn is discussed in relation to the role of CoQ in the membrane.Coenzyme Q (CoQ) is a component of the mitochondrial respiratory chain which carries out additional membrane functions, such as acting as an antioxidant. The location of CoQ in the membrane and the interaction with the phospholipid bilayer is still a subject of debate. The interaction of CoQ in the oxidized (ubiquinone-10) and reduced (ubiquinol-10) state with membrane model systems of 1,2-dielaidoyl-sn-glycero-3-phosphoethanolamine (Ela2Gro-P-Etn) has been studied by means of differential scanning calorimetry (DSC), 31P-nuclear magnetic resonance (31P-NMR) and small angle X-ray diffraction (SAXD). Ubiquinone-10 did not visibly affect the lamellar gel to lamellar liquid-crystalline phase transition of Ela2Gro-P-Etn, but it clearly perturbed the multicomponent lamellar liquid-crystalline to lamellar gel phase transition of the phospholipid. The perturbation of both transitions was more effective in the presence of ubiquinol-10. A location of CoQ forming head to head aggregates in the center of the Ela2Gro-P-Etn bilayer with the polar rings protruding toward the phospholipid acyl chains is suggested. The formation of such aggregates are compatible with the strong hexagonal HII phase promotion ability found for CoQ. This ability was evidenced by the shifting of the lamellar to hexagonal HII phase transition to lower temperatures and by the appearance of the characteristic hexagonal HII 31P-NMR resonance and SAXD pattern at temperatures at which the pure Ela2Gro-P-Etn is still organized in extended bilayer structures. The influence of CoQ on the thermotropic properties and phase behavior of Ela2Gro-P-Etn is discussed in relation to the role of CoQ in the membrane.
Author Gómez‐Fernández, Juan C.
Llamas, Maria A.
Aranda, Francisco J.
Author_xml – sequence: 1
  givenname: Juan C.
  surname: Gómez‐Fernández
  fullname: Gómez‐Fernández, Juan C.
– sequence: 2
  givenname: Maria A.
  surname: Llamas
  fullname: Llamas, Maria A.
– sequence: 3
  givenname: Francisco J.
  surname: Aranda
  fullname: Aranda, Francisco J.
BackLink https://www.ncbi.nlm.nih.gov/pubmed/10092859$$D View this record in MEDLINE/PubMed
BookMark eNqNkF1LwzAUhoNM3If-BemVd635aJPmQkHHpsJAxHkd0iSlGW0zm45t_npbN0G82lUOOc95k_OMwaB2tQEgQDBCMKa3qwjFBIeIYBYhznkEIYI82p2B0aEBCRmAUXcbh5gndAjG3q8ghJRTdgGGCEKO04SPwGxZmMDWrWmkaq2rA5cHypn6a1-Z4C3Y2rYI1oXz60K2Vu9L0xaydqWsbG2CylRZI2vjL8F5Lktvro7nBHzMZ8vpc7h4fXqZPixCRWjCQ4YVJbkhOEdMa8LTOFEqhZTlDGmVYc2wTmGquZQZk5pTzDVSjOVxKrEmOZmAm0PuunGfG-NbUVmvTFl2n3AbL7r1Yso47cDrI7jJKqPFurGVbPbid_EOSA-Aapz3jcn_IKJ3LFaiVyl6x6J3LH4ci103ev9vVNlW9vLaRtrylIC7Q8DWlmZ_8sNiPnt87yryDW8glhs
CitedBy_id crossref_primary_10_1111_j_1751_1097_2007_00221_x
crossref_primary_10_1016_j_bbamem_2006_06_012
crossref_primary_10_1016_S1367_5931_99_00035_6
crossref_primary_10_1152_physrev_00040_2023
crossref_primary_10_1021_la8016084
crossref_primary_10_15171_apb_2018_001
crossref_primary_10_1021_jp802215s
crossref_primary_10_1021_jp066130x
crossref_primary_10_1016_j_ultramic_2007_04_009
crossref_primary_10_1007_s00249_015_1031_z
crossref_primary_10_1021_jp011001w
crossref_primary_10_1016_j_bbamem_2018_02_015
crossref_primary_10_1021_jp8102468
crossref_primary_10_1007_s10973_006_7916_4
crossref_primary_10_1016_j_bbamem_2016_02_034
crossref_primary_10_1016_j_bpc_2009_10_009
crossref_primary_10_1021_bi060615u
crossref_primary_10_1021_la025837h
crossref_primary_10_1016_j_chemphyslip_2004_04_007
crossref_primary_10_1016_j_envexpbot_2005_05_001
crossref_primary_10_1080_00268970010010204
crossref_primary_10_1016_j_freeradbiomed_2021_05_021
crossref_primary_10_1016_j_jdermsci_2006_12_011
crossref_primary_10_1016_S0005_2736_99_00034_6
crossref_primary_10_1016_j_bbamem_2017_03_021
crossref_primary_10_1016_S0005_2736_01_00426_6
crossref_primary_10_1021_ac8015856
ContentType Journal Article
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7X8
DOI 10.1046/j.1432-1327.1999.00109.x
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
MEDLINE - Academic
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
MEDLINE - Academic
DatabaseTitleList CrossRef

MEDLINE
MEDLINE - Academic
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Anatomy & Physiology
Chemistry
EISSN 1432-1033
EndPage 746
ExternalDocumentID 10092859
10_1046_j_1432_1327_1999_00109_x
FEBS109
Genre article
Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID -DZ
-~X
.55
.GA
.GJ
.Y3
10A
1OC
24P
29G
31~
36B
3O-
4.4
51W
51X
52N
52O
52P
52R
52S
52T
52W
52X
53G
5GY
5HH
5LA
5RE
66C
7PT
8-1
8-4
8-5
930
A01
A03
AAEVG
AAHHS
AAZKR
ABDBF
ABDPE
ABEFU
ABJNI
ACCFJ
ACFBH
ACGFS
ACMXC
ACNCT
ACUHS
ACXQS
ADBBV
ADIZJ
ADZOD
AEEZP
AEIMD
AEQDE
AEUQT
AFBPY
AFPWT
AFZJQ
AI.
AIWBW
AJBDE
ALMA_UNASSIGNED_HOLDINGS
ALUQN
AMBMR
BAWUL
BY8
C45
CAG
CO8
COF
CS3
D-7
D-F
DIK
E3Z
EAD
EAP
EAS
EAU
EBB
EBC
EBD
EBS
EBX
EJD
EMB
EMK
EMOBN
EST
ESX
EX3
F00
F01
F04
F5P
G-S
GODZA
GX1
HZI
IH2
IHE
IPNFZ
L7B
LH4
LP6
LP7
LW6
MVM
O9-
OBS
OHT
OVD
P4B
P4D
QB0
RIG
ROL
SDH
SUPJJ
SV3
TEORI
TR2
TUS
UB1
VH1
WH7
WOW
WQJ
WRC
WXI
X7M
XG1
Y6R
YFH
YSK
YUY
ZGI
ZXP
AAYXX
ADXHL
AETEA
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
PKN
1OB
7X8
AAMMB
AEFGJ
AGXDD
AIDQK
AIDYY
ID FETCH-LOGICAL-c3659-72c63fe32f17dd39845cc8067f71dcb2d72d808d9aab7ad9629d1c77f48a2d3f3
IEDL.DBID 24P
ISSN 0014-2956
IngestDate Fri Sep 05 09:42:48 EDT 2025
Wed Feb 19 02:33:29 EST 2025
Thu Apr 24 23:09:58 EDT 2025
Tue Jul 01 01:02:28 EDT 2025
Wed Jan 22 16:23:05 EST 2025
IsPeerReviewed true
IsScholarly true
Issue 3
Language English
License http://onlinelibrary.wiley.com/termsAndConditions#vor
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c3659-72c63fe32f17dd39845cc8067f71dcb2d72d808d9aab7ad9629d1c77f48a2d3f3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 10092859
PQID 69646796
PQPubID 23479
PageCount 8
ParticipantIDs proquest_miscellaneous_69646796
pubmed_primary_10092859
crossref_primary_10_1046_j_1432_1327_1999_00109_x
crossref_citationtrail_10_1046_j_1432_1327_1999_00109_x
wiley_primary_10_1046_j_1432_1327_1999_00109_x_FEBS109
ProviderPackageCode CITATION
AAYXX
PublicationCentury 1900
PublicationDate February 1999
1999-02-00
1999-Feb
19990201
PublicationDateYYYYMMDD 1999-02-01
PublicationDate_xml – month: 02
  year: 1999
  text: February 1999
PublicationDecade 1990
PublicationPlace Oxford, UK
PublicationPlace_xml – name: Oxford, UK
– name: England
PublicationTitle European journal of biochemistry
PublicationTitleAlternate Eur J Biochem
PublicationYear 1999
Publisher Blackwell Science Ltd
Publisher_xml – name: Blackwell Science Ltd
SSID ssj0006967
Score 1.5460443
Snippet Coenzyme Q (CoQ) is a component of the mitochondrial respiratory chain which carries out additional membrane functions, such as acting as an antioxidant. The...
SourceID proquest
pubmed
crossref
wiley
SourceType Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 739
SubjectTerms 31P‐nuclear magnetic resonance
Calorimetry, Differential Scanning
coenzyme Q
differential scanning calorimetry
Lipid Bilayers - chemistry
lipid polymorphism
Magnetic Resonance Spectroscopy
Models, Molecular
Phosphatidylethanolamines - chemistry
Phospholipids - chemistry
Temperature
Thermodynamics
Ubiquinone - analogs & derivatives
Ubiquinone - chemistry
Ubiquinone - pharmacology
X-Ray Diffraction
Title The interaction of coenzyme Q with phosphatidylethanolamine membranes
URI https://onlinelibrary.wiley.com/doi/abs/10.1046%2Fj.1432-1327.1999.00109.x
https://www.ncbi.nlm.nih.gov/pubmed/10092859
https://www.proquest.com/docview/69646796
Volume 259
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Na9wwEBUhPaSXkmbTdtsm0aH05mBLsmQd07BLCCQktAt7E7Iks4faXvYDuvn1nZG9S5fmEHLzRTK8p4-Z0cwbQr6BB8BEcGliubOJcI4npcxZkvHS-eBhXadYKHx3L28m4naaT_v8J6yF6fQhdgE33BnxvMYNbsuuC0ka1W1xk3OclCksuYuyk6m-BHvyDVbaYhsHJh52p7LUstPPzETCwCnos3q2L5zPzbR_Vf1nf-6bs_E-Gh-Td70hSa865t-Tg9CckMFVA050vaHfaUztjDHzE3J0vW3rNiAjWBgURSIWXUkDbSvq2tA8bepAHynGZel81i7nM-DMb4DWmW3A_60BMFqHGiCD0_GUTMajX9c3Sd9LIXFc5jpRzEleBc6qTHnPdSFy5wq4qiqVeVcyr5gv0sJra0tlvZZM-8wpVYnCMs8r_oEcNm0TPhHKhQhZsCwvFfiSqtBCaZYHrZyQQRd6SNQWNuN6oXHsd_HbxAdvIaPDwZlBwA0CbiLg5s-QZLuR805s4wVjLrbMGEASnzsAhna9NMC4wCjZkHzsCPtnzlSjcN-QyMjgi39mxqMfP-Hr82sHfiFvO90HzIf5Sg5Xi3U4A6tmVZ7H5foXF2rogA
linkProvider Wiley-Blackwell
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB6h9lAuiD6ABUp9QNxSEtux42Nb7WrpS1Rtpd6sxHa0B5Ks-pBYfj0zTnbVqhwqbrnYkb7x2PP8BuAregBcBpcmpXBlIp0TSaVynmSicj54PNcpNQqfnavptTy-yW-GcUDUC9PzQ6wCbqQZ8b4mBaeA9PchLTlouaBduaaeu8g7mZp9NCjXJZrpVN_H5c_VtayM6gk0M5lw9AqGsp5livNfOz19q54ZoE_t2fggTd7Cm8GSZAe96DfhVWi3YPugRS-6WbBvLNZ2xqD5FmwcLee6bcMYTwYjlojbvqeBdTVzXWj_LJrALhgFZtl81t3NZyg0v0C5zsoWHeAGEWNNaBAzvB534HoyvjqaJsMwhcQJlZtEc6dEHQSvM-29MIXMnSvwrap15l3Fvea-SAtvyrLSpTeKG585rWtZlNyLWryDtbZrwwdgQsqQhZLnlUZnUhdGasPzYLSTKpjCjEAvYbNuYBqngRe_bMx4SxU9DsEtAW4JcBsBt79HkK1Wznu2jRes2VtKxiKSlO9AGLqHO4sSlxQmG8H7XmCP9kwNMfeNQEUJvvhndjI-vMSvj_-7cA82pldnp_b0x_nJJ3jdk0BQccxnWLu_fQi7aOLcV1_i0f0Ly1br8w
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT9wwEB4hkFouVYGWbgvFh6q30MR27PjIY1eUtoiqIHGzEtvRHkiy4iF1-fXMONlVUXtAveViR_rGM57nZ4BPGAFwGVyalMKViXROJJXKeZKJyvng8VynNCj840ydXMrTq_xq6H-iWZieH2KZcCPNiPaaFHzm6y9DVXJQckGbck0jd5F2MjX76E-uUe2PlJTL86VVVkb1_JmZTDgGBUNXz6LC-a-dnl5Vf_mfT93ZeB9NXsOrwZFkB73kN2AltJuwddBiEN3M2WcWWztjznwTXh4tnnXbgjEeDEYkETf9SAPraua60D7Mm8B-MsrLstm0u51NUWZ-jmKdli3Gvw0CxprQIGRoHd_A5WR8cXSSDG8pJE6o3CSaOyXqIHidae-FKWTuXIFXVa0z7yruNfdFWnhTlpUuvVHc-MxpXcui5F7U4i2stl0b3gETUoYslDyvNMaSujBSG54Ho51UwRRmBHoBm3UD0Ti9d3FtY8FbqhhwCG4JcEuA2wi4_T2CbLly1pNtPGPN3kIyFpGkcgfC0N3fWpS4pCzZCLZ7gf2xZ2qIuG8EKkrw2T-zk_HhL_x6_78L9-DF-fHEfv969u0DrPcUENQaswOrdzf3YRcdnLvqYzy5j1Zi6xw
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=The+interaction+of+coenzyme+Q+with+phosphatidylethanolamine+membranes&rft.jtitle=European+journal+of+biochemistry&rft.au=G%C3%B3mez-Fern%C3%A1ndez%2C+J+C&rft.au=Llamas%2C+M+A&rft.au=Aranda%2C+F+J&rft.date=1999-02-01&rft.issn=0014-2956&rft.volume=259&rft.issue=3&rft.spage=739&rft_id=info:doi/10.1046%2Fj.1432-1327.1999.00109.x&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0014-2956&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0014-2956&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0014-2956&client=summon