DB code: M00062

RLCP classification 10.100012.100.10200 : Electron transfer
10.12100.110.10080 : Electron transfer
10.100110.100.10300 : Electron transfer
CATH domain 1.20.210.10 : Cytochrome C Oxidase; Chain A Catalytic domain
2.60.40.420 : Immunoglobulin-like Catalytic domain
1.10.287.90 : Helix Hairpins
1.10.287.70 : Helix Hairpins
1.20.120.80 : Four Helix Bundle (Hemerythrin (Met), subunit A)
1.20.5.160 : Single alpha-helices involved in coiled-coils or other helix-helix interfaces
E.C. 1.9.3.1
CSA 1ar1
M-CSA 1ar1
MACiE

CATH domain Related DB codes (homologues)
1.20.210.10 : Cytochrome C Oxidase; Chain A M00194
2.60.40.420 : Immunoglobulin-like T00215 T00216 M00115 M00194

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
P08306 Cytochrome c oxidase subunit 2
Oxidase aa(3) subunit 2
EC 1.9.3.1
Cytochrome c oxidase polypeptide II
Cytochrome aa3 subunit 2
PF00116 (COX2)
PF02790 (COX2_TM)
[Graphical View]
P06030 Cytochrome c oxidase subunit 3
EC 1.9.3.1
Cytochrome c oxidase polypeptide III
Cytochrome aa3 subunit 3
Oxidase aa(3) subunit 3
PF00510 (COX3)
[Graphical View]
P77921 Cytochrome c oxidase subunit 4
EC 1.9.3.1
Cytochrome c oxidase polypeptide IV
Cytochrome aa3 subunit 4
PF07835 (COX4_pro_2)
[Graphical View]
P98002 Cytochrome c oxidase subunit 1-beta
EC 1.9.3.1
Cytochrome c oxidase polypeptide I-beta
Cytochrome aa3 subunit 1-beta
PF00115 (COX1)
[Graphical View] 		YP_915727.1 (Protein)
NC_008686.1 (DNA/RNA sequence)

KEGG enzyme name
cytochrome-c oxidase
cytochrome oxidase
cytochrome a3
cytochrome aa3
Warburg's respiratory enzyme
indophenol oxidase
indophenolase
complex IV (mitochondrial electron transport)
ferrocytochrome c oxidase
NADH cytochrome c oxidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P98002 COX1B_PARDE 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. Cell inner membrane, Multi-pass membrane protein. Binds 1 copper B ion per subunit. Binds 2 heme groups per subunit.
P08306 COX2_PARDE 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. Cell inner membrane, Multi-pass membrane protein. Binds 2 copper A ions per subunit.
P06030 COX3_PARDE 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. Cell inner membrane, Multi-pass membrane protein.
P77921 COX4_PARDE 4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O. Cell inner membrane, Single-pass membrane protein.

KEGG Pathways
Map code Pathways E.C.
MAP00190 Oxidative phosphorylation

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00070 C00032 C00032 C00034 C00126 C00007 C00080 C00125 C00001
E.C.
Compound Copper Heme A Heme A3 Manganese Ferrocytochrome c O2 H+ Ferricytochrome c H2O
Type heavy metal aromatic ring (with nitrogen atoms),carboxyl group,heavy metal aromatic ring (with nitrogen atoms),carboxyl group,heavy metal heavy metal amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide group others others amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide group H2O
ChEBI 28694
 30052
 28694
 30052
 		17627
 26355
 17627
 26355
 		17627
 26355
 17627
 26355
 		18291
 35154
 18291
 35154
 		15379
 26689
 27140
 15379
 26689
 27140
 		15378
 15378
 		15377
 15377
PubChem 23978
 23978
 		23930
 23930
 		977
 977
 		1038
 1038
 		22247451
 962
 22247451
 962
1ar1A Bound:_CU Bound:HEA_1 Bound:HEA_2 Analogue:_MG Unbound Unbound Unbound
1qleA Bound:_CU Bound:HEA_1 Bound:HEA_2 Bound:_MN Unbound Unbound Unbound
1ar1B01 Bound:2x_CU Unbound Unbound Unbound Unbound Unbound Unbound
1qleB01 Bound:CUA Unbound Unbound Unbound Unbound Unbound Unbound
1ar1B02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qleB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qleC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qleC02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qleD Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [10], [26]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ar1A ASP 124;GLU 278;TYR 280;HIS 325;LYS 354 HIS 94;HIS 413(Heme A);HIS 411(Heme A3);HIS 276;TYR 280;HIS 325;HIS 326(Copper B);HIS 403;ASP 404(Manganese);GLU 56;HIS 59;GLY 61;GLN 63(Calcium) PHE 412;ARG 473;ARG 474
1qleA ASP 124;GLU 278;TYR 280;HIS 325;LYS 354 HIS 94;HIS 413(Heme A);HIS 411(Heme A3);HIS 276;TYR 280;HIS 325;HIS 326(Copper B);HIS 403;ASP 404(Manganese);GLU 56;HIS 59;GLY 61;GLN 63(Calcium) PHE 412;ARG 473;ARG 474
1ar1B01 TRP 121 HIS 181;CYS 216;CYS 220;MET 227(Copper A1);CYS 216;GLU 218;CYS 220;HIS 224(Copper A2);GLU 218;SER 217(Manganese)
1qleB01 TRP 121 HIS 181;CYS 216;CYS 220;MET 227(Copper A1);CYS 216;GLU 218;CYS 220;HIS 224(Copper A2);GLU 218;SER 217(Manganese)
1ar1B02
1qleB02
1qleC01
1qleC02
1qleD

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
Fig.5
[10]
Fig.5, p.666-668
[11]
Fig.1
[14]
p.463-464
[16]
Fig.5, p.13827-13828
[17]
p.10550-10552
[18]
Fig.4, p.2473-2475
[21]
p.828-832, Fig.13
[22]
Fig.1, p.719-720
[23]
Fig.1
[24]
Fig.1, Fig.6, p.371-373
[25]
[26]
Fig.6, p.102-106
[27]
[32]
Fig.6, p.987-988
[34]
Fig.1
[37]
p.6-7
[43]
Fig.1
[45]
p.51-59

References
[1]
Resource
Comments
Medline ID
PubMed ID 6307293
Journal Biochem Biophys Res Commun
Year 1983
Volume 113
Pages 575-80
Authors Yanagita Y, Sone N, Kagawa Y
Title Proton pumping and oxidase activity of thermophilic cytochrome oxidase remain after its extensive proteolysis.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2883179
Journal J Biochem (Tokyo)
Year 1986
Volume 100
Pages 1465-70
Authors Sone N
Title Measurement of proton pump activity of the thermophilic bacterium PS3 and Nitrobacter agilis at the cytochrome oxidase level using total membrane and heptyl thioglucoside.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8407882
Journal J Biochem (Tokyo)
Year 1993
Volume 114
Pages 88-95
Authors Yumoto I, Takahashi S, Kitagawa T, Fukumori Y, Yamanaka T
Title The molecular features and catalytic activity of CuA-containing aco3-type cytochrome c oxidase from a facultative alkalophilic Bacillus.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8068652
Journal Biochemistry
Year 1994
Volume 33
Pages 9731-40
Authors Haltia T, Semo N, Arrondo JL, Goni FM, Freire E
Title Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7577945
Journal Biochemistry
Year 1995
Volume 34
Pages 13565-9
Authors Echabe I, Haltia T, Freire E, Goni FM, Arrondo JL
Title Subunit III of cytochrome c oxidase influences the conformation of subunits I and II: an infrared study.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 7779804
Journal Biochemistry
Year 1995
Volume 34
Pages 7586-92
Authors Hosler JP, Espe MP, Zhen Y, Babcock GT, Ferguson-Miller S
Title Analysis of site-directed mutants locates a non-redox-active metal near the active site of cytochrome c oxidase of Rhodobacter sphaeroides.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 7727443
Journal Biochemistry
Year 1995
Volume 34
Pages 5824-30
Authors Lappalainen P, Watmough NJ, Greenwood C, Saraste M
Title Electron transfer between cytochrome c and the isolated CuA domain: identification of substrate-binding residues in cytochrome c oxidase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 7632682
Journal Biochemistry
Year 1995
Volume 34
Pages 9819-25
Authors Wang J, Takahashi S, Hosler JP, Mitchell DM, Ferguson-Miller S, Gennis RB, Rousseau DL
Title Two conformations of the catalytic site in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 7552705
Journal Nat Struct Biol
Year 1995
Volume 2
Pages 842-6
Authors Ostermeier C, Iwata S, Ludwig B, Michel H
Title Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase.
Related PDB
Related UniProtKB
[10]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID 95379947
PubMed ID 7651515
Journal Nature
Year 1995
Volume 376
Pages 660-9
Authors Iwata S, Ostermeier C, Ludwig B, Michel H
Title Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans.
Related PDB
Related UniProtKB P98002 P08306 P06030 P77921
[11]
Resource
Comments
Medline ID
PubMed ID 8718868
Journal Biochemistry
Year 1996
Volume 35
Pages 10776-83
Authors Hosler JP, Shapleigh JP, Mitchell DM, Kim Y, Pressler MA, Georgiou C, Babcock GT, Alben JO, Ferguson-Miller S, Gennis RB
Title Polar residues in helix VIII of subunit I of cytochrome c oxidase influence the activity and the structure of the active site.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8547262
Journal Biochemistry
Year 1996
Volume 35
Pages 824-8
Authors Mitchell DM, Adelroth P, Hosler JP, Fetter JR, Brzezinski P, Pressler MA, Aasa R, Malmstrom BG, Alben JO, Babcock GT, Gennis RB, Ferguson-Miller S
Title A ligand-exchange mechanism of proton pumping involving tyrosine-422 of subunit I of cytochrome oxidase is ruled out.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8825522
Journal Curr Biol
Year 1996
Volume 6
Pages 36-8
Authors Gennis RB, Ferguson-Miller S
Title Protein structure: proton-pumping oxidases.
Related PDB
Related UniProtKB
[14]
Resource
Comments REVIEW
Medline ID 96391941
PubMed ID 8794157
Journal Curr Opin Struct Biol
Year 1996
Volume 6
Pages 460-6
Authors Ostermeier C, Iwata S, Michel H
Title Cytochrome c oxidase.
Related PDB
Related UniProtKB P98002
[15]
Resource
Comments
Medline ID
PubMed ID 8955368
Journal FEBS Lett
Year 1996
Volume 397
Pages 303-7
Authors Lubben M, Gerwert K
Title Redox FTIR difference spectroscopy using caged electrons reveals contributions of carboxyl groups to the catalytic mechanism of haem-copper oxidases.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 9374859
Journal Biochemistry
Year 1997
Volume 36
Pages 13824-9
Authors Adelroth P, Ek MS, Mitchell DM, Gennis RB, Brzezinski P
Title Glutamate 286 in cytochrome aa3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen.
Related PDB
Related UniProtKB
[17]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
Medline ID 98021406
PubMed ID 9380672
Journal Proc Natl Acad Sci U S A
Year 1997
Volume 94
Pages 10547-53
Authors Ostermeier C, Harrenga A, Ermler U, Michel H
Title Structure at 2.7 A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment.
Related PDB 1ar1
Related UniProtKB P98002 P08306
[18]
Resource
Comments
Medline ID
PubMed ID 9485395
Journal Biochemistry
Year 1998
Volume 37
Pages 2470-6
Authors Adelroth P, Gennis RB, Brzezinski P
Title Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 9922138
Journal Biochemistry
Year 1998
Volume 37
Pages 17726-34
Authors Karlin S, Zhu ZY, Karlin KD
Title Extended metal environments of cytochrome c oxidase structures.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 9585552
Journal Biochemistry
Year 1998
Volume 37
Pages 7378-89
Authors Salgado J, Warmerdam G, Bubacco L, Canters GW
Title Understanding the electronic properties of the CuA site from the soluble domain of cytochrome c oxidase through paramagnetic 1H NMR.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 9893941
Journal Biochimie
Year 1998
Volume 80
Pages 821-36
Authors Papa S, Capitanio N, Villani G, Capitanio G, Bizzoca A, Palese LL, Carlino V, De Nitto E
Title Cooperative coupling and role of heme a in the proton pump of heme-copper oxidases.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 9533684
Journal Biophys J
Year 1998
Volume 74
Pages 708-21
Authors Kannt A, Lancaster CR, Michel H
Title The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 9492306
Journal Eur J Biochem
Year 1998
Volume 251
Pages 367-73
Authors Witt H, Malatesta F, Nicoletti F, Brunori M, Ludwig B
Title Cytochrome-c-binding site on cytochrome oxidase in Paracoccus denitrificans.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 9538216
Journal J Biochem (Tokyo)
Year 1998
Volume 123
Pages 369-75
Authors Iwata S
Title Structure and function of bacterial cytochrome c oxidase.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 9478966
Journal J Biol Chem
Year 1998
Volume 273
Pages 5132-6
Authors Witt H, Malatesta F, Nicoletti F, Brunori M, Ludwig B
Title Tryptophan 121 of subunit II is the electron entry site to cytochrome-c oxidase in Paracoccus denitrificans. Involvement of a hydrophobic patch in the docking reaction.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 9443344
Journal Proteins
Year 1998
Volume 30
Pages 100-7
Authors Hofacker I, Schulten K
Title Oxygen and proton pathways in cytochrome c oxidase.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 9660711
Journal Science
Year 1998
Volume 280
Pages 1712-3
Authors Gennis RB
Title Cytochrome c oxidase: one enzyme, two mechanisms?
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 10029521
Journal Biochemistry
Year 1999
Volume 38
Pages 2287-94
Authors Villani G, Capitanio N, Bizzoca A, Palese LL, Carlino V, Tattoli M, Glaser P, Danchin A, Papa S
Title Effects of site-directed mutagenesis of protolytic residues in subunit I of Bacillus subtilis aa3-600 quinol oxidase. Role of lysine 304 in proton translocation.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 10481041
Journal FEBS Lett
Year 1999
Volume 458
Pages 83-6
Authors Hellwig P, Soulimane T, Buse G, Mantele W
Title Similarities and dissimilarities in the structure-function relation between the cytochrome c oxidase from bovine heart and from Paracoccus denitrificans as revealed by FT-IR difference spectroscopy.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 10462045
Journal FEBS Lett
Year 1999
Volume 456
Pages 365-9
Authors Pfitzner U, Kirichenko A, Konstantinov AA, Mertens M, Wittershagen A, Kolbesen BO, Steffens GC, Harrenga A, Michel H, Ludwig B
Title Mutations in the Ca2+ binding site of the Paracoccus denitrificans cytochrome c oxidase.
Related PDB
Related UniProtKB
[31]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10559205
Journal J Biol Chem
Year 1999
Volume 274
Pages 33296-9
Authors Harrenga A, Michel H
Title The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction.
Related PDB 1qle
Related UniProtKB
[32]
Resource
Comments COVALENT BOND
Medline ID 99268331
PubMed ID 10338009
Journal Protein Sci
Year 1999
Volume 8
Pages 985-90
Authors Buse G, Soulimane T, Dewor M, Meyer HE, Bluggel M
Title Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase.
Related PDB
Related UniProtKB P98002
[33]
Resource
Comments
Medline ID
PubMed ID 10891065
Journal Biochemistry
Year 2000
Volume 39
Pages 7863-7
Authors Backgren C, Hummer G, Wikstrom M, Puustinen A
Title Proton translocation by cytochrome c oxidase can take place without the conserved glutamic acid in subunit I.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 10828950
Journal Biochemistry
Year 2000
Volume 39
Pages 6365-72
Authors Riistama S, Puustinen A, Verkhovsky MI, Morgan JE, Wikstrom M
Title Binding of O(2) and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans.
Related PDB
Related UniProtKB
[35]
Resource
Comments
Medline ID
PubMed ID 11352755
Journal Biochemistry
Year 2001
Volume 40
Pages 6180-9
Authors Gupta S, Warne A, Saraste M, Mazumdar S
Title pH-induced conformational transition in the soluble CuA domain of Paracoccus denitrificans cytochrome oxidase.
Related PDB
Related UniProtKB
[36]
Resource
Comments
Medline ID
PubMed ID 11425307
Journal Biochemistry
Year 2001
Volume 40
Pages 7806-11
Authors Vos MH, Lipowski G, Lambry JC, Martin JL, Liebl U
Title Dynamics of nitric oxide in the active site of reduced cytochrome c oxidase aa3.
Related PDB
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 11341911
Journal Biochim Biophys Acta
Year 2001
Volume 1544
Pages 1-9
Authors Abramson J, Svensson-Ek M, Byrne B, Iwata S
Title Structure of cytochrome c oxidase: a comparison of the bacterial and mitochondrial enzymes.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 11513871
Journal FEBS Lett
Year 2001
Volume 503
Pages 142-6
Authors Kannt A, Ostermann T, Muller H, Ruitenberg M
Title Zn(2+) binding to the cytoplasmic side of Paracoccus denitrificans cytochrome c oxidase selectively uncouples electron transfer and proton translocation.
Related PDB
Related UniProtKB
[39]
Resource
Comments
Medline ID
PubMed ID 11374571
Journal Spectrochim Acta A Mol Biomol Spectrosc
Year 2001
Volume 57A
Pages 1123-31
Authors Hellwig P, Rost B, Mantele W
Title Redox dependent conformational changes in the mixed valence form of the cytochrome c oxidase from p. The reorganization of glutamic acid 278 is coupled to the electron transfer from/to heme a and the binuclear center. denitrificans.
Related PDB
Related UniProtKB
[40]
Resource
Comments
Medline ID
PubMed ID 12071962
Journal Eur J Biochem
Year 2002
Volume 269
Pages 2980-8
Authors Drosou V, Malatesta F, Ludwig B
Title Mutations in the docking site for cytochrome c on the Paracoccus heme aa3 oxidase. Electron entry and kinetic phases of the reaction.
Related PDB
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 11950842
Journal J Biol Chem
Year 2002
Volume 277
Pages 22402-6
Authors Giuffre A, Barone MC, Brunori M, D'Itri E, Ludwig B, Malatesta F, Muller HW, Sarti P
Title Nitric oxide reacts with the single-electron reduced active site of cytochrome c oxidase.
Related PDB
Related UniProtKB
[42]
Resource
Comments
Medline ID
PubMed ID 11825904
Journal J Biol Chem
Year 2002
Volume 277
Pages 13563-8
Authors Pinakoulaki E, Pfitzner U, Ludwig B, Varotsis C
Title The role of the cross-link His-Tyr in the functional properties of the binuclear center in cytochrome c oxidase.
Related PDB
Related UniProtKB
[43]
Resource
Comments
Medline ID
PubMed ID 11986672
Journal Nature
Year 2002
Volume 417
Pages 99-102
Authors Ruitenberg M, Kannt A, Bamberg E, Fendler K, Michel H
Title Reduction of cytochrome c oxidase by a second electron leads to proton translocation.
Related PDB
Related UniProtKB
[44]
Resource
Comments
Medline ID
PubMed ID 11870867
Journal Proteins
Year 2002
Volume 47
Pages 75-85
Authors Flock D, Helms V
Title Protein--protein docking of electron transfer complexes: cytochrome c oxidase and cytochrome c.
Related PDB
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 12783267
Journal Rev Physiol Biochem Pharmacol
Year 2003
Volume 147
Pages 47-74
Authors Richter OM, Ludwig B
Title Cytochrome c oxidase--structure, function, and physiology of a redox-driven molecular machine.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 15518562
Journal Biochemistry
Year 2004
Volume 43
Pages 14118-27
Authors Pilet E, Nitschke W, Rappaport F, Soulimane T, Lambry JC, Liebl U, Vos MH
Title NO binding and dynamics in reduced heme-copper oxidases aa3 from Paracoccus denitrificans and ba3 from Thermus thermophilus.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 15041635
Journal Biophys J
Year 2004
Volume 86
Pages 1873-89
Authors Olkhova E, Hutter MC, Lill MA, Helms V, Michel H
Title Dynamic water networks in cytochrome C oxidase from Paracoccus denitrificans investigated by molecular dynamics simulations.
Related PDB
Related UniProtKB
[48]
Resource
Comments
Medline ID
PubMed ID 14672950
Journal J Biol Chem
Year 2004
Volume 279
Pages 10293-303
Authors Paumann M, Lubura B, Regelsberger G, Feichtinger M, Kollensberger G, Jakopitsch C, Furtmuller PG, Peschek GA, Obinger C
Title Soluble CuA domain of cyanobacterial cytochrome c oxidase.
Related PDB
Related UniProtKB

Comments
This enzyme, cytochrome c oxidase, is so-called "Complex IV (mitochondrial electron transport).
Although this enzyme is partially homologous to that from T. thermophilus (Bacteria) (M00194 in EzCatDB), the subunit/domain compositions seem to be slightly different from the counterpart enzyme.
Bacterial enzymes are composed of 3 or 4 subunits. Of the three or four subunits, subunits I and II form the functional core of the enzyme complex. The subunit I binds a copper ion (CuB), two heme groups (heme A and heme A3), along with manganese ion bound at the interface with the subunit II. The subunit II binds a binuclear copper ion pair, CuA. Heme A3 and CuB form a binuclear centre for O2 reduction.
Taken together, this enzyme catalyzes the following reactions, electron transfers and dioxygen reduction, coupling with proton pumping.
4 cyt c(red) + 8 H+(in) + O2 = 4 cyt c(ox) + 2 H2O + 4 H+(out)
According to the literature [7], [10], [45], this enzyme catalyzes the following reactions:
(A) Electron transfer from cytochrome c (substrate;ferrocytochrome c) to CuA (subunit II):
(B) Electron transfer from CuA (subunit II) to heme A (subunit I):
(C) Electron transfer from heme A (subunit I) to binculear center (heme A3 & CuB) (subunit I):
(D) Reduction of dioxygen (O2) to H2O (at the binuclear center):
(E) Proton pump
According to the literature [10], the following reaction proceeds as follows:
(A) Electron transfer from cytochrome c (substrate;ferrocytochrome c) to CuA (subunit II):
(A1) Indirect transfer through Trp121 (subunit II) to Met227 bound to CuA-1 (see [10], [25]).
(B) Electron transfer from CuA (subunit II) to heme A (subunit I):
(B1) Indirect transfer through His224 (subunit II), mainchain carbonyl oxygen of Arg473 and mainchain amide of Arg474 (subunit I), and propionate (carboxylate) group of heme A.
(C) Electron transfer from heme A (subunit I) to binculear center (heme A3 & CuB) (subunit I):
(C1) Indirect transfer through His413 bound to heme A iron, mainchain of Phe412, and His411 bound to heme A3 iron (see [10]).

Created Updated
2004-04-19 2009-02-26