Information on EC 7.1.1.9 - cytochrome-c oxidase and Organism(s) Bos taurus and UniProt Accession P00415

P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184

-

-

?

amidopyrine + H2O2

?

-

-

?

benzidine + H2O2

?

-

-

?

diaminobenzidine + H2O2

?

-

-

?

ferrocytochrome c + O2

ferricytochrome c + H2O

4 entries

ferrocytochrome c + O2 + H+

ferricytochrome c + H2O

5 entries

melatonin + H2O2

?

-

-

?

o-dianisidine + H2O2

?

-

-

?

p-phenylenediamine + H2O2

?

-

-

?

peroxynitrite

NO + O22-

-

enzyme must be fully reduced, proposed reaction

396126

-

396126

?

reduced Bos taurus cytochrome c + O2 + H+

oxidized Bos taurus cytochrome c + H2O

-

-

?

reduced cytochrome c + O2 + H+

oxidized cytochrome c + H2O

tetramethylbenzidine + H2O2

?

-

-

?

additional information

?

-

ferrocytochrome c + O2

ferricytochrome c + H2O

-

terminal enzyme of the electron transport chain. The glucagon receptor/G-protein/c-AMP pathway regulates enzyme activity

-

?

ferrocytochrome c + O2 + H+

ferricytochrome c + H2O

3 entries

additional information

?

-

-

cytochrome c oxidase is an efficient energy transducer that reduces oxygen to water and converts the released chemical energy into an electrochemical membrane potential. As a true proton pump, the enzyme translocates protons across the membrane against this potential

724436

-

?

heme

heme a

Heme a3

Cu

Cu2+

Fe

Fe2+

-

interaction of inhibitor nitric oxide is either with ferrous heme iron or oxidized copper, but not both simultaneously. The affinity of NO for the oxygen-binding ferrous heme site is 0.2 nM

Fe3+

contains iron

Mg

Zn

additional information

-

variation of metal content with purification procedure

396049

ATP

-

the ATP-inhibition of CcO is only effective at very high ATP/ADP ratios (above 50) in the mitochondrial matrix or at low concentrations of ferrocytochrome c

azide

-

CN-

CO

cyanide

-

Dicyclohexylcarbodiimide

-

395995

ethylene glycol

-

inhibits by reducing electron flow between cytochrome a and cytochrome a3

F-

-

NaN3

-

nitric oxide

NO

peroxynitrite

-

0.1 mM, complete inhibition

phosphate

-

Sulfide

-

theophylline

-

at therapeutic concentrations used for asthma relief, theophylline causes inhibition of the lung enzyme and decreases cellular ATP levels, suggesting a mechanism for its clinical action

Triton X-100

-

Tumor necrosis factor alpha

-

leads to an ca. 60% reduction in CcO activity in hepatocyte homogenates. Shows no direct effect on CcO activity using purified CcO. CcO isolated after tumor necrosis factor alpha treatment shows tyrosine phosphorylation on CcO catalytic subunit I and is ca. 50 and 70% inhibited at high cytochrome c concentrations in the presence of allosteric activator ADP and inhibitor ATP, respectively

-

Zn2+

additional information

-

(3Z)-3-[(4-hydroxy-3,5-dimethoxyphenyl)methylidene]-1-[3-[(5-hydroxy-4-oxo-2-phenyl-4H-1-benzopyran-7-yl)oxy]propyl]-1,3-dihydro-2H-indol-2-one

-

compound developed for clipping cyanide from the enzyme and restoring its normal function. The binding constant with CN- is 230000 per M and its ED50 for restoring the cyanide bound CcOX activity in 10 min is 16 microM. The compound interacts with CN- over the pH range 5-10

ADP

-

NO

-

geminates recombination in mitochondrial CcO. Can accommodate only one NO molecule in its active site

691038

Tween 80

-

1% slight stimulation

Tween-20

-

711289

additional information

3 entries

-

0.00005 - 0.077

ferrocytochrome c

16 entries

0.09

o-Dianisidine

-

at 1 mM H2O2

0.001

O2

-

1 - 500

ferrocytochrome c

4 entries

additional information

-

study of reaction kinetics assuming a fast protonic phase with a proton transfer to H291 and a slow process with a proton transfer to OH-group of binuclear catalytic site. Comparison with kinetics of enzyme from Rhodobacter spaeroides and Paracoccus denitrificans

672326

-

0.018

-

additional information

-

CuA depleted enzyme shows 15% activity of native and 75% activity of p-(hydroxymercuri)benzoate modified enzyme

6

-

6 - 6.5

-

25

-

40

-

-

UniProt

P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184

-

kidney

P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184

-

fibroblast

P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184

-

-

-

396035, 396052, 396064, 396065, 396078, 659507, 711289

longissimus lumborum

-

comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity in different types of muscle

muscle

-

psoas major, longissimus lumborum, superficial semimembranosus, deep semimembranosus, and semitendinosus muscle, comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity

psoas major

-

comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity in different types of muscle

semimembranosus

-

superficial and deep semimembranosus, comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity in different types of muscle

semitendinosus

-

comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity in different types of muscle

-

additional information

-

mammalian tissue-specific isoforms

396032

membrane

mitochondrial inner membrane

P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184

-

P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184

-

-

5743

mitochondrial membrane

-

31966

396118, 742086, 742135

mitochondrion

4 entries

metabolism

-

cytochrome c oxidase is the terminal enzyme in the respiratory electron transport chain of mitochondria. It catalyzes the reduction of oxygen to water to generate the electrochemical proton gradient across the mitochondrial membrane that powers the production of ATP. The enzyme takes up four electrons from the positively charged P side (outside) of the membrane and four protons from the negatively charged N side (inside) for the reduction of dioxygen to two water molecules

724436

P00415 pBLAST

COX3_BOVIN

261

6

29933

Swiss-Prot

Show Sequence

Secretory Pathway (Reliability: 3)

15 entries

10068

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

10670

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

12436

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

17153

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

200000

-

heart, monomeric enzyme, deoxycholate solubilized, hydrodynamic measurements

210000

gel filtration

26049

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

29918

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

326000

-

dimeric enzyme complex, sedimentation equilibrium centrifugation

396039

350000

-

dimeric form, Triton X-100 solubilized, hydrodynamic measurements

5441

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

56993

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

6244

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

6350

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

8480

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

9419

-

I, II, III, IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, VIII, 1 * 56993 + 1 * 26049 + 1 * 29918 + 1 * 17153 + 1 * 12436 + 1 * 10670 + 1 * 9419 + 1 * 10068 + 1 * 8480 + 1 * 5441 + 1 * 6244 + 1 * 6350 + 1 * 4962, heart, 13 subunits, nomenclature system of subunits according to Kadenbach et. al, BRENDA reference 396096 (PubMed-ID 6303162), and literature cited therein, other nomenclature systems, amino acid sequences

395999, 396000, 396002, 396050, 396058, 396098, 396109

monomer

1 210000, calculated from sequence

755271

oligomer

additional information

17 entries

phospholipoprotein

3 entries

phosphoprotein

-

cAMP-dependent tyrosine phosphorylation of subunit I inhibits cytochrome c oxidase activity

additional information

-

comparison of two oxidized states of enzyme, the state as isolated in the fast form, and the form obtained immediately after oxidation of fully reduced cytochrome-c oxidase with O2. No observable differences are found between these two states

674661

concentration of the purified enzyme by Amicon ultrafiltration in 0.3-1 mM or 10 mM sodium phosphate buffer, dimeric in crystal lattice

-

396106

enzyme from heart can be crystallized in hexagonal, tetragonal and orthorhombic forms

-

396133

in complex with CO, NO, and CN-

726369

microbatch method, at pH 7.3 and 5.7, using 3% (w/v) polyethylene glycol 1500 as precipitant

-

741541

monomeric bovine cytochrome c oxidase with bound cytochrome c, microbatch method

-

743264

oxidized and reduced structures of monomer with resolutions of 1.85 and 1.95 A, respectively. A hydrogen bond network of water molecules is formed at the entry surface of the proton transfer pathway, in monomeric CcO, whereas this network is altered in dimeric CcO. Phospholipid structures are found with the protein complex, two cardiolipins are found at the interface region of the supercomplex

755271

room temperature, pH 6.8, damage-free structure in the carbon monoxide-bound state at a resolution of 2.3 A. In the femtosecond X-ray crystallography structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of about 142°. In the synchrotron structure, the Fe-CO bond is cleaved. CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by about 0.38 Å. Ligand binding to the heme a3 iron in the femtosecond X-ray crystallography structure is associated with an allosteric structural transition

755261

two-dimensional crystals by insertion of the enzyme into preformed lipid vesicles

-

396066

X-ray structure of heart cytochrome c oxidase in the fully oxidized state

-

396132

37 - 61

-

the half-life of the enzyme at 37°C is 0.4 h, the dissociation of subunit III and/or VIIa is responsible for temperature-induced inactivation of the enzyme at 61°C

742086

additional information

depletion of lipids causes inactivation

-

dimethyl sulfoxide

-

no inactivation

dimethylformamide

-

no inactivation

Ethanol

-

60%, no inactivation

Ethylene glycol

-

60%, no inactivation

Methanol

-

60%, no inactivation

propanediol

-

no inactivation

propanol

-

60%, no inactivation

-60°C, 100 mM phosphate buffer, pH 7.4, 1% Tween 80

-

-70°C

-

-70°C, concentrated solution

-

396037

-80°C, 20 mM Tris-Cl buffer, pH 7.4, 250 mM sucrose, 2 mM EDTA

-

4°C, 0.2 M phosphate buffer, 2% cholate, decrease of solubility during long term storage

-

396092

by small-scale immunopurification

P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184

-

affinity chromatography on horse heart ctochrome c

-

by gel filtration

-

by small-scale immunopurification

P00396, P00415, P00423, P00426, P00428, P00429, P00430, P04038, P07470, P07471, P10175, P13183, P13184

HiTrap Q column chromatography

-

742086

cDNA of subunits IV, Vb, VIa, VIb, VIc, VIIb, VIIc, and VIII

-

396032

proton pumping activity of cytochrome c oxidase reconstituted in phospholipid vesicles

-

396067

reconstitution into dimyristoylphosphatidylcholine vesicles

-

396107

reconstitution into phospholipid vesicles

-

396028

reconstitution into phospholipid vesicles in the presence of hydrophobic poly(vinyl alkanoate) polymers

-

396028

reconstitution methods

-

reconstitution of proton pumping activity

-

396063

analysis

-

cytochrome c oxidase modified electrodes can be used to distinguish amino acid sequence variations in proteins such as cytochrome c. This has potential relevance as a diagnostic for disease states, characterization of electron transfer reactions of cytochrome c isolated from ischemic and control hearts

drug development

medicine

nutrition

-

in beef muscles psoas major, longissimus lumborum, superficial semimembranosus, deep semimembranosus, and semitendinosus, comparison of cytochrome c oxidase activity, instrumental and visual colour, metmyoglobin-reducing activity, and total reducing activity. Colour stability among muscles is variable and metmyoglobin-reducing activity is more useful than total reducing activity for explaining the role of reducing activity in muscle-colour stability

additional information

29 entries

395995

Brunori, M.; Antonini, G.; Malatesta, F.; Sarti, P.; Wilson, M.T.

Cytochrome-c oxidase. Subunit structure and proton pumping

Eur. J. Biochem.

169

1-8

1987

Bacteria, Bos taurus, Mammalia, Paracoccus denitrificans

2445564

395999

Capaldi, R.A.; Malatesta, F.; Darley-Usmar, V.M.

Structure of cytochrome c oxidase

Biochim. Biophys. Acta

726

135-148

1983

Bos taurus, Mammalia

6307356

396000

Kadenbach, B.; Merle, P.

On the function of multiple subunits of cytochrome c oxidase from higher eukaryotes

FEBS Lett.

135

1-11

1981

Bos taurus, eukaryota, Rattus norvegicus

6274682

396001

Wikstr�m, M.; Krab, K.; Saraste, M.

Proton-translocating cytochrome complexes

Annu. Rev. Biochem.

50

623-655

1981

Bacteria, Bos taurus, eukaryota, Neurospora crassa

6267990

396002

Azzi, A.

Cytochrome c oxidase. Towards a clarification of its structure, interactions and mechanism

Biochim. Biophys. Acta

594

231-252

1980

Bos taurus, Saccharomyces cerevisiae, eukaryota, Homo sapiens, Neurospora crassa, Rattus norvegicus

6264952

396003

Ludwig, B.

Heme aa3-type cytochrome c oxidases from bacteria

Biochim. Biophys. Acta

594

177-189

1980

Bacteria, Bos taurus, Thermus thermophilus, Paracoccus denitrificans, Nitrobacter winogradskyi, Starkeya novella, Bacillus sp. PS3

6263325

396004

Malmstr�m, B.G.

Cytochrome c oxidase. Structure and catalytic activity

Biochim. Biophys. Acta

549

281-303

1979

Bos taurus, Saccharomyces cerevisiae

228720

396006

Caughey, W.S.; Wallace, W.J.; Volpe, J.A.; Yoshikawa, S.

Cytochrome c oxidase

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

13

299-344

1976

Bos taurus, Saccharomyces cerevisiae

-

396007

Nicholls, P.; Chance, B.

Cytochrome c oxidase

Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York

479-534

1974

Bos taurus, eukaryota

-

396009

Robinson, N.C.; Dale, M.P.; Talbert, L.H.

Subunit analysis of bovine cytochrome c oxidase by reverse phase high performance liquid chromatography

Arch. Biochem. Biophys.

281

239-244

1990

Bos taurus

2168156

396014

Han, S.; Ching, Y.C.; Rousseau, D.L.

Primary intermediate in the reaction of oxygen with fully reduced cytochrome c oxidase

Proc. Natl. Acad. Sci. USA

87

2491-2495

1990

Bos taurus

2157201

396016

�blad, M.; Selin, E.; Malmstr�m, B.; Strid, L.; Aasa, R.; Malmstr�m, B.G.

Analytical characterization of cytochrome oxidase preparations with regard to metal and phospholipid contents, peptide composition and catalytic activity

Biochim. Biophys. Acta

975

267-270

1989

Bos taurus

2545268

396019

Scott, R.A.

X-ray absorption spectroscopic investigations of cytochrome c oxidase structure and function

Annu. Rev. Biophys. Biophys. Chem.

18

137-158

1989

Bos taurus

2544193

396028

Sarti, P.; Antonini, G.; Malatesta, F.; Vallone, B.; Villaschi, S.; Brunori, M.; Hider, R.C.; Hamed, K.

Reconstitution of cytochrome c oxidase in phospholipid vesicles containing polyvinylic polymers

Biochem. J.

257

783-787

1989

Bos taurus

2539096

396032

Lomax, M.I.; Grossman, L.I.

Tissue-specific genes for respiratory proteins [published erratum appears in Trends Biochem Sci 1990 Jun;15(6):217]

Trends Biochem. Sci.

14

501-503

1989

Bos taurus, Homo sapiens, Rattus norvegicus

2560276

396033

Naqui, A.; Powers, L.; Lundeen, M.; Constantinescu, A.; Chance, B.

On the environment of zinc in beef heart cytochrome c oxidase: an x-ray absorption study

J. Biol. Chem.

263

12342-12345

1988

Bos taurus

2842329

396035

Bombelka, E.; Richter, F.W.; Stroh, A.; Kadenbach, B.

Analysis of the Cu, Fe, and Zn contents in cytochrome C oxidases from different species and tissues by proton-induced X-ray emission (PIXE)

Biochem. Biophys. Res. Commun.

140

1007-1014

1986

Bos taurus, Rattus norvegicus, Sus scrofa

3022731

396037

Einarsdottir, O.; Caughey, W.S.

Zinc is a constituent of bovine heart cytochrome c oxidase preparations

Biochem. Biophys. Res. Commun.

124

836-842

1984

Bos taurus

6095824

396038

Einarsdottir, O.; Caughey, W.S.

Bovine heart cytochrome c oxidase preparations contain high affinity binding sites for magnesium as well as for zinc, copper, and heme iron

Biochem. Biophys. Res. Commun.

129

840-847

1985

Bos taurus

2990471

396039

Georgevich, G.; Darley-Usmar, V.M.; Capaldi, R.A.

Electron transfer in monomeric forms of beef and shark heart cytochrome c oxidase

Biochemistry

22

1317-1322

1983

Bos taurus, Sphyrna lewini

6301544

396040

Steffens, G.J.; Buse, G.

Studies on cytochrome c oxidase, IV[1-3]. Primary structure and function of subunit II

Hoppe-Seyler's Z. Physiol. Chem.

360

613-619

1979

Bos taurus

220175

396041

Martin, C.T.; Scholes, C.P.; Chan, S.I.

On the nature of cysteine coordination to CuA in cytochrome c oxidase

J. Biol. Chem.

263

8420-8429

1988

Bos taurus

2836423

396043

Rich, P.R.; West, I.C.; Mitchell, P.

The location of CuA in mammalian cytochrome c oxidase

FEBS Lett.

233

25-30

1988

Bos taurus, Rattus norvegicus

2454843

396049

Yewey, G.L.; Caughey, W.S.

Metals of bovine heart cytochrome c oxidase

Ann. N. Y. Acad. Sci.

550

22-32

1988

Bos taurus

2854394

Brunori, M.; Antonini, G.; Malatesta, F.; Sarti, P.; Wilson, M.T.

Structure and function of cytochrome oxidase: a second look

Adv. Inorg. Biochem.

7

93-154

1987

Bacteria, Bos taurus, eukaryota

2821746

396052

Sinjorgo, K.M.C.; Durak, I.; Dekker, H.L.; Edel, C.M.; Hakvoort, T.B.M.; van Gelder, B.F.; Muijsers, A.O.

Bovine cytochrome c oxidases, purified from heart, skeletal muscle, liver and kidney, differ in the small subunits but show the same reaction kinetics with cytochrome c

Biochim. Biophys. Acta

893

251-258

1987

Bos taurus

3040092

396056

Li, M.P.; Gelles, J.; Chan, S.I.; Sullivan, R.J.; Scott, R.A.

Extended X-ray absorption fine structure of copper in CuA-depleted, p-(hydroxymercuri)benzoate-modified, and native cytochrome c oxidase

Biochemistry

26

2091-2095

1987

Bos taurus

3040080

396058

Capaldi, R.A.; Gonzales-Halphen, D.; Takamiya, S.

Sequence homologies and structural similarities between the polypeptides of yeast and beef heart cytochrome c oxidase

FEBS Lett.

207

11-17

1986

Bos taurus, Saccharomyces cerevisiae

3021525

396063

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Bos taurus

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