PDBsum entry 1ocr

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
Protein chains
514 a.a. *
227 a.a. *
261 a.a. *
144 a.a. *
109 a.a. *
98 a.a. *
84 a.a. *
79 a.a. *
73 a.a. *
58 a.a. *
49 a.a. *
47 a.a. *
43 a.a. *
HEA ×4
_NA ×2
_CU ×6
_ZN ×2
_MG ×2
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Bovine heart cytochromE C oxidase in the fully reduced state
Structure: CytochromE C oxidase. Chain: a, n. Synonym: ferrocytochrome c\:oxygen oxidoreductase. Other_details: this enzyme is a hybrid protein complex and is a homodimer. Fully reduced state.. CytochromE C oxidase. Chain: b, o. Synonym: ferrocytochrome c\:oxygen oxidoreductase. Other_details: this enzyme is a hybrid protein complex and
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: heart. Tissue: heart muscle. Organelle: mitochondrion. Organelle: mitochondrion
Biol. unit: 26mer (from PQS)
2.35Å     R-factor:   0.203     R-free:   0.247
Authors: T.Tsukihara,M.Yao
Key ref:
S.Yoshikawa et al. (1998). Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science, 280, 1723-1729. PubMed id: 9624044 DOI: 10.1126/science.280.5370.1723
07-Jul-98     Release date:   29-Jul-99    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P00396  (COX1_BOVIN) -  Cytochrome c oxidase subunit 1
514 a.a.
514 a.a.
Protein chains
Pfam   ArchSchema ?
P68530  (COX2_BOVIN) -  Cytochrome c oxidase subunit 2
227 a.a.
227 a.a.
Protein chains
Pfam   ArchSchema ?
P00415  (COX3_BOVIN) -  Cytochrome c oxidase subunit 3
261 a.a.
261 a.a.*
Protein chains
Pfam   ArchSchema ?
P00423  (COX41_BOVIN) -  Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
169 a.a.
144 a.a.
Protein chains
Pfam   ArchSchema ?
P00426  (COX5A_BOVIN) -  Cytochrome c oxidase subunit 5A, mitochondrial
152 a.a.
109 a.a.
Protein chains
Pfam   ArchSchema ?
P00428  (COX5B_BOVIN) -  Cytochrome c oxidase subunit 5B, mitochondrial
129 a.a.
98 a.a.
Protein chains
Pfam   ArchSchema ?
P07471  (CX6A2_BOVIN) -  Cytochrome c oxidase subunit 6A2, mitochondrial
97 a.a.
84 a.a.
Protein chains
Pfam   ArchSchema ?
P00429  (CX6B1_BOVIN) -  Cytochrome c oxidase subunit 6B1
86 a.a.
79 a.a.
Protein chains
Pfam   ArchSchema ?
P04038  (COX6C_BOVIN) -  Cytochrome c oxidase subunit 6C
74 a.a.
73 a.a.
Protein chains
Pfam   ArchSchema ?
P07470  (CX7A1_BOVIN) -  Cytochrome c oxidase subunit 7A1, mitochondrial
80 a.a.
58 a.a.
Protein chains
Pfam   ArchSchema ?
P13183  (COX7B_BOVIN) -  Cytochrome c oxidase subunit 7B, mitochondrial
80 a.a.
49 a.a.
Protein chains
Pfam   ArchSchema ?
P00430  (COX7C_BOVIN) -  Cytochrome c oxidase subunit 7C, mitochondrial
63 a.a.
47 a.a.
Protein chains
Pfam   ArchSchema ?
P10175  (COX8B_BOVIN) -  Cytochrome c oxidase subunit 8B, mitochondrial
70 a.a.
43 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chains A, N: E.C.  - Cytochrome-c oxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O
4 × ferrocytochrome c
Bound ligand (Het Group name = HEA)
matches with 50.00% similarity
+ O(2)
+ 4 × H(+)
= 4 × ferricytochrome c
+ 2 × H(2)O
      Cofactor: Cu cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   11 terms 
  Biological process     oxidation-reduction process   8 terms 
  Biochemical function     electron carrier activity     8 terms  


DOI no: 10.1126/science.280.5370.1723 Science 280:1723-1729 (1998)
PubMed id: 9624044  
Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.
S.Yoshikawa, K.Shinzawa-Itoh, R.Nakashima, R.Yaono, E.Yamashita, N.Inoue, M.Yao, M.J.Fei, C.P.Libeu, T.Mizushima, H.Yamaguchi, T.Tomizaki, T.Tsukihara.
Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site exchanges its effective accessibility to the matrix aqueous phase for one to the cytosolic phase concomitantly with a significant decrease in the pK of its carboxyl group, on reduction of the metal sites. The movement indicates the aspartate as the proton pumping site. A tyrosine acidified by a covalently linked imidazole nitrogen is a possible proton donor for the O2 reduction by the enzyme.
  Selected figure(s)  
Figure 2.
Fig. 2. Crystal structures of the Fe[a3]-Cu[B] site in the fully reduced CO-bound and fully oxidized azide-bound states and those of^ the Na^+/Ca^2+ and Mg^2+ sites. (F[o] F[c]) difference Fourier maps for CO bound at Fe[a3]^ at 3 level (A) and azide bridging between Fe[a3] and Cu[B]^ at 2.2 level (B) are given where the bound ligands and^ fixed waters are not included in the F[c] calculation. The difference^ electron density maps at 4 level (1 = 0.0436e^-/Å^3) for the Na^+/Ca^2+ site (C) and for the Mg^2+ site (D). Violet, purple, and blue balls are the positions^ of Na^+, Mg^2+, and water, respectively.
Figure 3.
Fig. 3. Redox-coupled conformational change in the segment from Gly^49 to Asn^55. The conformation of the segment in the fully oxidized form is^ stereoscopically shown in red, and that in the fully reduced form^ in green. The yellow structure denotes subunit II with no redox-coupled^ conformational change.
  The above figures are reprinted by permission from the AAAs: Science (1998, 280, 1723-1729) copyright 1998.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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Circular dichroism spectra of cytochrome c oxidase.
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21368144 I.von der Hocht, J.H.van Wonderen, F.Hilbers, H.Angerer, F.Macmillan, and H.Michel (2011).
Interconversions of P and F intermediates of cytochrome c oxidase from Paracoccus denitrificans.
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21205904 J.Liu, L.Qin, and S.Ferguson-Miller (2011).
Crystallographic and online spectral evidence for role of conformational change and conserved water in cytochrome oxidase proton pump.
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PDB codes: 3om3 3oma 3omi 3omn
21545285 S.Yoshikawa, K.Muramoto, and K.Shinzawa-Itoh (2011).
Proton-pumping mechanism of cytochrome C oxidase.
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20936199 V.L.Davidson (2011).
Generation of protein-derived redox cofactors by posttranslational modification.
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Crystal structures of all-alpha type membrane proteins.
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20385840 K.Muramoto, K.Ohta, K.Shinzawa-Itoh, K.Kanda, M.Taniguchi, H.Nabekura, E.Yamashita, T.Tsukihara, and S.Yoshikawa (2010).
Bovine cytochrome c oxidase structures enable O2 reduction with minimization of reactive oxygens and provide a proton-pumping gate.
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PDB codes: 3ag1 3ag2 3ag3 3ag4
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Structures of membrane proteins.
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A spectroscopic investigation of a tridentate Cu-complex mimicking the tyrosine-histidine cross-link of cytochrome C oxidase.
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19548766 A.Y.Smirnov, L.G.Mourokh, and F.Nori (2009).
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19303362 B.Kadenbach, R.Ramzan, and S.Vogt (2009).
Degenerative diseases, oxidative stress and cytochrome c oxidase function.
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19164527 H.Aoyama, K.Muramoto, K.Shinzawa-Itoh, K.Hirata, E.Yamashita, T.Tsukihara, T.Ogura, and S.Yoshikawa (2009).
A peroxide bridge between Fe and Cu ions in the O2 reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump.
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PDB codes: 2zxw 3abl 3abm
19894768 J.P.Collman, A.Dey, C.J.Barile, S.Ghosh, and R.A.Decréau (2009).
Inhibition of electrocatalytic O(2) reduction of functional CcO models by competitive, non-competitive, and mixed inhibitors.
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19541624 J.P.Collman, A.Dey, Y.Yang, S.Ghosh, and R.A.Decréau (2009).
O2 reduction by a functional heme/nonheme bis-iron NOR model complex.
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20007376 J.P.Collman, S.Ghosh, A.Dey, and R.A.Decréau (2009).
Using a functional enzyme model to understand the chemistry behind hydrogen sulfide induced hibernation.
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19218360 K.Kobayashi, S.Tagawa, and T.Mogi (2009).
Intramolecular electron transfer processes in Cu(B)-deficient cytochrome bo studied by pulse radiolysis.
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19584547 K.Kobayashi, S.Tagawa, and T.Mogi (2009).
Electron transfer processes in subunit I mutants of cytochrome bo quinol oxidase in Escherichia coli.
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19348907 L.Geren, B.Durham, and F.Millett (2009).
Chapter 28 Use of ruthenium photoreduction techniques to study electron transfer in cytochrome oxidase.
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19810693 M.E.Mahoney, A.Oliver, O.Einarsdóttir, and J.P.Konopelski (2009).
Synthesis of a cyclic pentapeptide mimic of the active site His-Tyr cofactor of cytochrome c oxidase.
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19623382 P.E.Siegbahn, and M.R.Blomberg (2009).
A combined picture from theory and experiments on water oxidation, oxygen reduction and proton pumping.
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19463779 T.Egawa, H.J.Lee, R.B.Gennis, S.R.Yeh, and D.L.Rousseau (2009).
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19187032 T.Hayashi, M.T.Lin, K.Ganesan, Y.Chen, J.A.Fee, R.B.Gennis, and P.Moënne-Loccoz (2009).
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18509049 A.V.Pisliakov, P.K.Sharma, Z.T.Chu, M.Haranczyk, and A.Warshel (2008).
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19004768 D.G.Isom, B.R.Cannon, C.A.Castañeda, A.Robinson, and B.García-Moreno (2008).
High tolerance for ionizable residues in the hydrophobic interior of proteins.
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18459161 D.Horn, and A.Barrientos (2008).
Mitochondrial copper metabolism and delivery to cytochrome c oxidase.
  IUBMB Life, 60, 421-429.  
18418633 E.A.Berry, and F.A.Walker (2008).
Bis-histidine-coordinated hemes in four-helix bundles: how the geometry of the bundle controls the axial imidazole plane orientations in transmembrane cytochromes of mitochondrial complexes II and III and related proteins.
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18664577 E.A.Gorbikova, I.Belevich, M.Wikström, and M.I.Verkhovsky (2008).
The proton donor for O-O bond scission by cytochrome c oxidase.
  Proc Natl Acad Sci U S A, 105, 10733-10737.  
18798008 F.M.Ho (2008).
Uncovering channels in photosystem II by computer modelling: current progress, future prospects, and lessons from analogous systems.
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17949262 I.Belevich, and M.I.Verkhovsky (2008).
Molecular mechanism of proton translocation by cytochrome C oxidase.
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18928258 J.A.Fee, D.A.Case, and L.Noodleman (2008).
Toward a chemical mechanism of proton pumping by the B-type cytochrome c oxidases: application of density functional theory to cytochrome ba3 of Thermus thermophilus.
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18632561 J.P.Collman, A.Dey, R.A.Decreau, Y.Yang, A.Hosseini, E.I.Solomon, and T.A.Eberspacher (2008).
Interaction of nitric oxide with a functional model of cytochrome c oxidase.
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18956030 J.P.Collman, and R.A.Decréau (2008).
Functional biomimetic models for the active site in the respiratory enzyme cytochrome c oxidase.
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18155154 J.Xu, and G.A.Voth (2008).
Redox-coupled proton pumping in cytochrome c oxidase: further insights from computer simulation.
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18830692 M.A.Sharpe, and S.Ferguson-Miller (2008).
A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases.
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18294138 M.S.Muntyan, and D.A.Bloch (2008).
Study of redox potential in cytochrome c covalently bound to terminal oxidase of alkaliphilic Bacillus pseudofirmus FTU.
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18771294 M.S.Rogers, R.Hurtado-Guerrero, S.J.Firbank, M.A.Halcrow, D.M.Dooley, S.E.Phillips, P.F.Knowles, and M.J.McPherson (2008).
Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen.
  Biochemistry, 47, 10428-10439.
PDB codes: 2vz1 2vz3
18729107 N.Yeung, and Y.Lu (2008).
One heme, diverse functions: using biosynthetic myoglobin models to gain insights into heme-copper oxidases and nitric oxide reductases.
  Chem Biodivers, 5, 1437-1448.  
18824464 S.E.Hart, C.J.Howe, K.Mizuguchi, and J.Fernandez-Recio (2008).
Docking of cytochrome c6 and plastocyanin to the aa3-type cytochrome c oxidase in the cyanobacterium Phormidium laminosum.
  Protein Eng Des Sel, 21, 689-698.  
18294124 V.B.Borisov (2008).
Interaction of bd-type quinol oxidase from Escherichia coli and carbon monoxide: heme d binds CO with high affinity.
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17514341 C.Dallacosta, W.A.Alves, A.M.da Costa Ferreira, E.Monzani, and L.Casella (2007).
A new dinuclear heme-copper complex derived from functionalized protoporphyrin IX.
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17895387 J.Treuffet, K.J.Kubarych, J.C.Lambry, E.Pilet, J.B.Masson, J.L.Martin, M.H.Vos, M.Joffre, and A.Alexandrou (2007).
Direct observation of ligand transfer and bond formation in cytochrome c oxidase by using mid-infrared chirped-pulse upconversion.
  Proc Natl Acad Sci U S A, 104, 15705-15710.  
17470809 K.Muramoto, K.Hirata, K.Shinzawa-Itoh, S.Yoko-o, E.Yamashita, H.Aoyama, T.Tsukihara, and S.Yoshikawa (2007).
A histidine residue acting as a controlling site for dioxygen reduction and proton pumping by cytochrome c oxidase.
  Proc Natl Acad Sci U S A, 104, 7881-7886.
PDB codes: 2eij 2eik 2eil 2eim 2ein
17668091 K.N.White, I.Sen, I.Szundi, Y.R.Landaverry, L.E.Bria, J.P.Konopelski, M.M.Olmstead, and O.Einarsdóttir (2007).
Synthesis and structural characterization of cross-linked histidine-phenol Cu(ii) complexes as cytochrome c oxidase active site models.
  Chem Commun (Camb), (), 3252-3254.  
17360500 K.Shimokata, Y.Katayama, H.Murayama, M.Suematsu, T.Tsukihara, K.Muramoto, H.Aoyama, S.Yoshikawa, and H.Shimada (2007).
The proton pumping pathway of bovine heart cytochrome c oxidase.
  Proc Natl Acad Sci U S A, 104, 4200-4205.  
17350588 M.H.Olsson, P.E.Siegbahn, M.R.Blomberg, and A.Warshel (2007).
Exploring pathways and barriers for coupled ET/PT in cytochrome c oxidase: a general framework for examining energetics and mechanistic alternatives.
  Biochim Biophys Acta, 1767, 244-260.  
18021062 P.Nicholls (2007).
The oxygenase-peroxidase theory of Bach and Chodat and its modern equivalents: change and permanence in scientific thinking as shown by our understanding of the roles of water, peroxide, and oxygen in the functioning of redox enzymes.
  Biochemistry (Mosc), 72, 1039-1046.  
18021063 P.R.Rich, and M.Iwaki (2007).
A comparison of catalytic site intermediates of cytochrome c oxidase and peroxidases.
  Biochemistry (Mosc), 72, 1047-1055.  
17277769 P.Syntichaki, K.Troulinaki, and N.Tavernarakis (2007).
eIF4E function in somatic cells modulates ageing in Caenorhabditis elegans.
  Nature, 445, 922-926.  
17375955 R.A.Decréau, J.P.Collman, Y.Yang, Y.Yan, and N.K.Devaraj (2007).
Syntheses of hemoprotein models that can be covalently attached onto electrode surfaces by click chemistry.
  J Org Chem, 72, 2794-2802.  
17997553 T.Hayashi, I.J.Lin, Y.Chen, J.A.Fee, and P.Moënne-Loccoz (2007).
Fourier transform infrared characterization of a CuB-nitrosyl complex in cytochrome ba3 from Thermus thermophilus: relevance to NO reductase activity in heme-copper terminal oxidases.
  J Am Chem Soc, 129, 14952-14958.  
17534481 X.Liang, D.J.Campopiano, and P.J.Sadler (2007).
Metals in membranes.
  Chem Soc Rev, 36, 968-992.  
17955155 Z.O.Wang, and D.D.Pollock (2007).
Coevolutionary patterns in cytochrome c oxidase subunit I depend on structural and functional context.
  J Mol Evol, 65, 485-495.  
16477525 A.C.Dalziel, C.D.Moyes, E.Fredriksson, and S.C.Lougheed (2006).
Molecular evolution of cytochrome c oxidase in high-performance fish (teleostei: Scombroidei).
  J Mol Evol, 62, 319-331.  
16761090 D.M.Popovic, and A.A.Stuchebrukhov (2006).
Two conformational states of Glu242 and pKas in bovine cytochrome c oxidase.
  Photochem Photobiol Sci, 5, 611-620.  
16804678 H.Li, J.Igarashi, J.Jamal, W.Yang, and T.L.Poulos (2006).
Structural studies of constitutive nitric oxide synthases with diatomic ligands bound.
  J Biol Inorg Chem, 11, 753-768.
PDB codes: 2g6h 2g6i 2g6j 2g6k 2g6l 2g6m 2g6n 2g6o
16598262 I.Belevich, M.I.Verkhovsky, and M.Wikström (2006).
Proton-coupled electron transfer drives the proton pump of cytochrome c oxidase.
  Nature, 440, 829-832.  
16791638 I.Bento, M.A.Carrondo, and P.F.Lindley (2006).
Reduction of dioxygen by enzymes containing copper.
  J Biol Inorg Chem, 11, 539-547.  
16789843 J.S.Winterle, and O.Einarsdóttir (2006).
Photoreactions of cytochrome C oxidase.
  Photochem Photobiol, 82, 711-719.  
17050688 L.Qin, C.Hiser, A.Mulichak, R.M.Garavito, and S.Ferguson-Miller (2006).
Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase.
  Proc Natl Acad Sci U S A, 103, 16117-16122.
PDB code: 2gsm
17023543 L.S.Busenlehner, L.Salomonsson, P.Brzezinski, and R.N.Armstrong (2006).
Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase.
  Proc Natl Acad Sci U S A, 103, 15398-15403.  
16614069 M.H.Olsson, and A.Warshel (2006).
Monte Carlo simulations of proton pumps: on the working principles of the biological valve that controls proton pumping in cytochrome c oxidase.
  Proc Natl Acad Sci U S A, 103, 6500-6505.  
16788913 M.R.Blomberg, and P.E.Siegbahn (2006).
Quantum chemistry applied to the mechanisms of transition metal containing enzymes -- cytochrome c oxidase, a particularly challenging case.
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16352525 M.Seigneuret (2006).
Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: conserved and variable structural domains in the tetraspanin superfamily.
  Biophys J, 90, 212-227.
PDB code: 2avz
16728506 M.W.Bowler, M.G.Montgomery, A.G.Leslie, and J.E.Walker (2006).
How azide inhibits ATP hydrolysis by the F-ATPases.
  Proc Natl Acad Sci U S A, 103, 8646-8649.
PDB codes: 2ck3 2lcd
16387770 O.Farver, E.Grell, B.Ludwig, H.Michel, and I.Pecht (2006).
Rates and Equilibrium of CuA to heme a electron transfer in Paracoccus denitrificans cytochrome c oxidase.
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16820845 R.P.Pesavento, D.A.Pratt, J.Jeffers, and W.A.van der Donk (2006).
Model studies of the Cu(B) site of cytochrome c oxidase utilizing a Zn(II) complex containing an imidazole-phenol cross-linked ligand.
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16373477 R.Schwartz, and J.King (2006).
Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure.
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16983380 S.J.Lippard (2006).
The inorganic side of chemical biology.
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16220142 A.E.Bednarski, S.C.Elgin, and H.B.Pakrasi (2005).
An inquiry into protein structure and genetic disease: introducing undergraduates to bioinformatics in a large introductory course.
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16037213 A.Jasaitis, F.Rappaport, E.Pilet, U.Liebl, and M.H.Vos (2005).
Activationless electron transfer through the hydrophobic core of cytochrome c oxidase.
  Proc Natl Acad Sci U S A, 102, 10882-10886.  
16127664 A.S.Fandiño, I.Rais, M.Vollmer, H.Elgass, H.Schägger, and M.Karas (2005).
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PDB code: 1ngk
14673090 T.Tsukihara, K.Shimokata, Y.Katayama, H.Shimada, K.Muramoto, H.Aoyama, M.Mochizuki, K.Shinzawa-Itoh, E.Yamashita, M.Yao, Y.Ishimura, and S.Yoshikawa (2003).
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A novel copper A containing menaquinol NO reductase from Bacillus azotoformans.
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Kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast.
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Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers.
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Glutamate 189 of the D1 polypeptide modulates the magnetic and redox properties of the manganese cluster and tyrosine Y(Z) in photosystem II.
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Nonlinear electron paramagnetic resonance studies of the interaction of cytochrome c oxidase with spin-labeled lipids in gel-phase membranes.
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Proton-coupled structural changes upon binding of carbon monoxide to cytochrome cd1: a combined flash photolysis and X-ray crystallography study.
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PDB code: 1dy7
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Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus.
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PDB code: 1ehk
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Primary structure of a novel subunit in ba3-cytochrome oxidase from Thermus thermophilus.
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Direct evidence for a tyrosine radical in the reaction of cytochrome c oxidase with hydrogen peroxide.
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10346904 I.A.Smirnova, P.Adelroth, R.B.Gennis, and P.Brzezinski (1999).
Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation.
  Biochemistry, 38, 6826-6833.  
10194374 J.P.Osborne, N.J.Cosper, C.M.Stälhandske, R.A.Scott, J.O.Alben, and R.B.Gennis (1999).
Cu XAS shows a change in the ligation of CuB upon reduction of cytochrome bo3 from Escherichia coli.
  Biochemistry, 38, 4526-4532.  
10320356 M.Fabian, and G.Palmer (1999).
Redox state of peroxy and ferryl intermediates in cytochrome c oxidase catalysis.
  Biochemistry, 38, 6270-6275.  
10557282 M.Fabian, W.W.Wong, R.B.Gennis, and G.Palmer (1999).
Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase.
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10216152 M.H.Vos, and J.L.Martin (1999).
Femtosecond processes in proteins.
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10026287 M.Lübben, A.Prutsch, B.Mamat, and K.Gerwert (1999).
Electron transfer induces side-chain conformational changes of glutamate-286 from cytochrome bo3.
  Biochemistry, 38, 2048-2056.  
10587446 M.R.Bratton, M.A.Pressler, and J.P.Hosler (1999).
Suicide inactivation of cytochrome c oxidase: catalytic turnover in the absence of subunit III alters the active site.
  Biochemistry, 38, 16236-16245.  
10353829 M.Ralle, M.L.Verkhovskaya, J.E.Morgan, M.I.Verkhovsky, M.Wikström, and N.J.Blackburn (1999).
Coordination of CuB in reduced and CO-liganded states of cytochrome bo3 from Escherichia coli. Is chloride ion a cofactor?
  Biochemistry, 38, 7185-7194.  
10026246 P.Hellwig, S.Grzybek, J.Behr, B.Ludwig, H.Michel, and W.Mäntele (1999).
Electrochemical and ultraviolet/visible/infrared spectroscopic analysis of heme a and a3 redox reactions in the cytochrome c oxidase from Paracoccus denitrificans: separation of heme a and a3 contributions and assignment of vibrational modes.
  Biochemistry, 38, 1685-1694.  
10571999 S.Hirota, T.Iwamoto, K.Tanizawa, O.Adachi, and O.Yamauchi (1999).
Spectroscopic characterization of carbon monoxide complexes generated for copper/topa quinone-containing amine oxidases.
  Biochemistry, 38, 14256-14263.  
10074355 S.Paula, A.Sucheta, I.Szundi, and O.Einarsdóttir (1999).
Proton and electron transfer during the reduction of molecular oxygen by fully reduced cytochrome c oxidase: a flow-flash investigation using optical multichannel detection.
  Biochemistry, 38, 3025-3033.  
10200174 S.Siletsky, A.D.Kaulen, and A.A.Konstantinov (1999).
Resolution of electrogenic steps coupled to conversion of cytochrome c oxidase from the peroxy to the ferryl-oxo state.
  Biochemistry, 38, 4853-4861.  
10449737 T.K.Das, C.M.Gomes, M.Teixeira, and D.L.Rousseau (1999).
Redox-linked transient deprotonation at the binuclear site in the aa(3)-type quinol oxidase from Acidianus ambivalens: implications for proton translocation.
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10563822 T.K.Das, M.Couture, H.C.Lee, J.Peisach, D.L.Rousseau, B.A.Wittenberg, J.B.Wittenberg, and M.Guertin (1999).
Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: evidence for ligation of tyrosine-63 (B10) to the heme.
  Biochemistry, 38, 15360-15368.  
10348620 T.L.Poulos, H.Li, and C.S.Raman (1999).
Heme-mediated oxygen activation in biology: cytochrome c oxidase and nitric oxide synthase.
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9922158 A.Sucheta, I.Szundi, and O.Einarsdóttir (1998).
Intermediates in the reaction of fully reduced cytochrome c oxidase with dioxygen.
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9788998 H.Michel (1998).
The mechanism of proton pumping by cytochrome c oxidasex127e comments]
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9748311 K.M.Broekemeier, C.K.Klocek, and D.R.Pfeiffer (1998).
Proton selective substate of the mitochondrial permeability transition pore: regulation by the redox state of the electron transport chain.
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9811847 M.Karpefors, P.Adelroth, Y.Zhen, S.Ferguson-Miller, and P.Brzezinski (1998).
Proton uptake controls electron transfer in cytochrome c oxidase.
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9860833 M.V.Ponamarev, and W.A.Cramer (1998).
Perturbation of the internal water chain in cytochrome f of oxygenic photosynthesis: loss of the concerted reduction of cytochromes f and b6.
  Biochemistry, 37, 17199-17208.  
9788983 R.B.Gennis (1998).
How does cytochrome oxidase pump protons?
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9922138 S.Karlin, Z.Y.Zhu, and K.D.Karlin (1998).
Extended metal environments of cytochrome c oxidase structures.
  Biochemistry, 37, 17726-17734.  
9893941 S.Papa, N.Capitanio, G.Villani, G.Capitanio, A.Bizzoca, L.L.Palese, V.Carlino, and E.De Nitto (1998).
Cooperative coupling and role of heme a in the proton pump of heme-copper oxidases.
  Biochimie, 80, 821-836.  
9772174 T.K.Das, C.Pecoraro, F.L.Tomson, R.B.Gennis, and D.L.Rousseau (1998).
The post-translational modification in cytochrome c oxidase is required to establish a functional environment of the catalytic site.
  Biochemistry, 37, 14471-14476.  
9914255 U.Ermler, W.Grabarse, S.Shima, M.Goubeaud, and R.K.Thauer (1998).
Active sites of transition-metal enzymes with a focus on nickel.
  Curr Opin Struct Biol, 8, 749-758.  
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