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Information on EC 7.1.1.4 - caldariellaquinol oxidase (H+-transporting)
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7.1.1.4 caldariellaquinol oxidase (H+-transporting)IUBMB Comments
A copper-containing cytochrome. The enzyme from thermophilic archaea is part of the terminal oxidase and catalyses the reduction of O2 to water, accompanied by the extrusion of protons across the cytoplasmic membrane.
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Word Map
- 7.1.1.4
- quinols
-
heme-copper
-
binuclear
- paracoccus
- acidocaldarius
-
maltoside
- n,n,n',n'-tetramethyl-p-phenylenediamine
- ambivalens
- acidianus
-
quinol-oxidizing
-
heme-heme
-
cyanide-resistant
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
2
+
+
n
=
2
+
2
+
n
Synonyms
aa3-type cytochrome oxidase, terminal quinol oxidase, soxabcd complex, cytochrome aa3-type oxidase, aa3-type quinol oxidase, cytochrome aa3-type quinol oxidase, aa3 quinol oxidase, terminal quinol:oxygen oxidoreductase, soxm terminal oxidase supercomplex, soxm supercomplex, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cytochrome aa3
cytochrome aa3-type oxidase
EC 1.10.3.13
-
-
formerly
-
SoxM
SoxM is part of a larger protein complex which also contains SoxC, but neither SoxA nor SoxB
SoxM supercomplex
terminal quinol oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 caldariellaquinol + O2 + n H+[side 1] = 2 caldariellaquinone + 2 H2O + n H+[side 2]
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
caldariellaquinol oxidase (H+-transporting)
A copper-containing cytochrome. The enzyme from thermophilic archaea is part of the terminal oxidase and catalyses the reduction of O2 to water, accompanied by the extrusion of protons across the cytoplasmic membrane.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3,5,6-tetrachlorobenzoquinol + oxidized dithiothreitol
?
-
-
-
-
?
menadiol + oxidized dithiothreitol
menadione + dithiothreitol
-
-
-
-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2
?
-
N,N,N',N'-tetramethyl-1,4-phenylenediamine-ascorbate dependent oxygen consumption
-
-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2 + n H+/in
?
P39480; P98004; P39479; P39477
the SoxABCD complex is a proton-pumping quinol oxidase. With N,N,N',N'-tetramethyl-1,4-phenylenediamine as a reductant, the SoxABCD complex reconstituted into liposomes generates a proton motive force. The purified SoxABCD oxidase does not react with cytochrome c or blue copper proteins such as halocyanine or azurin as electron donors. However, considerable turnover numbers are found with N,N,N',N'-tetramethyl-1,4-phenylenediamine or caldariellaquinol, confirming that in vivo the enzyme is acting as a quinol oxidase
-
-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine + oxidized dithiothreitol
?
-
the physiological electron donor of the SoxABCD complex is probably caldariellaquinol. Since caldariellaquinol is very hydrophobic and difficult to use in vitro, N,N,N',N'-tetramethyl-1,4-phenylenediamine is used as a convenient artificial substrate
-
-
?
additional information
?
-
-
starting with the ascorbate plus N,N,Nâ,N'-tetramethyl-p-phenylendiamine-reduced enzyme, intramolecular electron transfer within this complex is very rapid
-
-
?
2 caldariellaquinol + O2 + n H+[side 1]
2 caldariellaquinone + 2 H2O + n H+[side 2]
-
proposed overall intramolecular electron transfer scheme of the terminal oxidase supercomplex from Sulfolobus sp. strain 7: caldariellaquinol -> cytochrome b562 -> Rieske FeS center -> cytochrome a583-aa3 -> molecular oxygen
-
-
?
2 caldariellaquinol + O2 + n H+[side 1]
2 caldariellaquinone + 2 H2O + n H+[side 2]
-
proposed overall intramolecular electron transfer scheme of the terminal oxidase supercomplex from Sulfolobus sp. strain 7: caldariellaquinol -> cytochrome b562 -> Rieske FeS center -> cytochrome a583-aa3 -> molecular oxygen
-
-
?
4 ferrocytochrome c + O2 + 4 H+
4 ferricytochrome c + 2 H2O
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
enzymatic activity is monitored with reduced cytochrome c despite not being the natural substrate. Sulfolobus acidocaldarius does not contain any c-type cytochrome. However, it can be used for in vitro assays of the terminal oxidase moiety in the complex because electrons can be accepted form either sulfocyanin (SoxE) or from SoxH. SoxABCD does not react with cytochrome c. The tested activity is specific for the SoxM complex
-
-
?
caldariella quinol + O2 + n H+/in
caldariella quinone + H2O + n H+/out
P94117; P94118
-
-
-
?
caldariella quinol + O2 + n H+/in
caldariella quinone + H2O + n H+/out
-
isolated aa3 preparation does not oxidize cytochrome c
-
-
?
caldariella quinol + O2 + n H+/in
caldariella quinone + H2O + n H+/out
-
isolated aa3 preparation does not oxidize cytochrome c
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
P94117; P94118
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
the enzyme cannot oxidize reduced cytochrome c
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
the major quinone in aerobically grown Acidianus ambivalens is caldariellaquinone, which is a thiophenobenzoquinone present in the Sulfolobales. The detergent-solubilized enzyme oxidizes caldariellaquinol at a high rate and with high specificity. The heme a3 formyl group undergoes a redox-induced change in its hydrogen bonding, at a much faster rate in the membrane-integrated than in the purified enzyme. It is proposed that a functional role of the bound quinone, in addition to being involved in the electron transfer chain, is to facilitate the conformational changes in the enzyme required for its proper function. In addition, the nature of the redox-linked changes is studied in relation to the physiological conditions of Acidianus ambivalens, and a redox/proton translocation coupling site near the heme a3 formyl group is postulated
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
two kinetic phases are observed. The first phase is attributed to binding of O2 to heme a3 and oxidation of both hemes forming the peroxy intermediate. The second phase is associated with proton uptake from solution and it is attributed to formation of the oxo-ferryl state, the final state in the absence of quinol. In the presence of bound caldariella quinol, heme a is re-reduced by caldariella quinol with a rate of 670/s, followed by transfer of the fourth electron to the binuclear center with a rate of 50/s. Thus the quinol donates electrons to heme a, followed by intramolecular transfer to the binuclear center
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
two kinetic phases are observed. The first phase is attributed to binding of O2 to heme a3 and oxidation of both hemes forming the peroxy intermediate. The second phase is associated with proton uptake from solution and it is attributed to formation of the oxo-ferryl state, the final state in the absence of quinol. In the presence of bound caldariella quinol, heme a is re-reduced by caldariella quinol with a rate of 670/s, followed by transfer of the fourth electron to the binuclear center with a rate of 50/s. Thus the quinol donates electrons to heme a, followed by intramolecular transfer to the binuclear center
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
P94117; P94118
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
function as a redox-driven proton pump, within the SoxGFE assembly of the supercomplex acting as a caldariella-quinol:sulfocyanin oxidoreductase
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
the physiological electron donor of the SoxABCD complex is probably caldariellaquinol. Since caldariellaquinol is very hydrophobic and difficult to use in vitro, N,N,N',N'-tetramethyl-1,4-phenylenediamine is used as an artificial substrate
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
highest activity with the physiological substrate caldariella quinol. When reconstituted into archaeal lipids, the quinol oxidase is able to generate and maintain a proton-motive force at temperatures approximately equivalent to the physiological growth conditions of this organism
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
P39480; P98004; P39479; P39477
the SoxABCD complex is a proton-pumping quinol oxidase. With N,N,N',N'-tetramethyl-1,4-phenylenediamine as a reductant, the SoxABCD complex reconstituted into liposomes generates a proton motive force. The purified SoxABCD oxidase does not react with cytochrome c or blue copper proteins such as halocyanine or azurine as electron donors. However, considerable turnover numbers are found with N,N,N',N'-tetramethyl-1,4-phenylenediamine or caldariella quinol, confirming that in vivo the enzyme is acting as a quinol oxidase
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
the SoxM-complex can oxidize the electron donor horseheart cytochrome c as well as caldariellaquinol. Based on genetic information it is suggested that the complex provides two proton pumping sites. However a preparation of liposomes with tetraether lipids together with the complex is not sufficient to perform proton pumping experiments
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
highest activity with the physiological substrate caldariella quinol. When reconstituted into archaeal lipids, the quinol oxidase is able to generate and maintain a proton-motive force at temperatures approximately equivalent to the physiological growth conditions of this organism
-
-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine hydrochloride + O2
?
-
-
-
-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine hydrochloride + O2
?
-
-
-
-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine hydrochloride + O2
?
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
caldariella quinol + O2 + n H+/in
caldariella quinone + H2O + n H+/out
P94117; P94118
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
P94117; P94118
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
P94117; P94118
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
-
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
function as a redox-driven proton pump, within the SoxGFE assembly of the supercomplex acting as a caldariella-quinol:sulfocyanin oxidoreductase
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
the physiological electron donor of the SoxABCD complex is probably caldariellaquinol. Since caldariellaquinol is very hydrophobic and difficult to use in vitro, N,N,N',N'-tetramethyl-1,4-phenylenediamine is used as an artificial substrate
-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome
-
the active respiratory terminal oxidase segment of Sulfolobus sp. strain 7 contains one non-CO-reactive b-type cytochrome (b562) and two different a-type cytochromes (a583 and aa3), in addition to one copper and a Rieske-type FeS cluster, which, as a whole, function as an active caldariellaquinol oxidase supercomplex
-
heme
-
a three-redox-centers enzyme. The enzyme has two heme with apparent redox potentials 215 mV and 415 mV at pH 5.4, and a heme a3-CuB center
heme
-
hemeprotein. The single subunit (38000-40000 Da) contains two heme a molecules. The redox potentials of the heme centres are +220 mV and +370 mV, respectively. One heme is a heme-a3 centre
heme
-
hemoprotein, contains two heme A molecules, one heme is a heme a3-centre, presence of a low-spin and a high-spin heme species
heme
P39480; P98004; P39479; P39477
the complex contains four haems A. Two haems belong to the 'cytochrome oxidase' part of the complex and two are probably bound to be apocytochrome b (SoxC) and responsible for the 586 nm absorption peak
heme
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
the enzyme contains 2 heme As and 2 heme B (b and b3)
heme
P39480; P98004; P39479; P39477
the enzyme contains four heme a redox centers. The EPR spectra indicate the presence of three low spin and one high spin heme species, the latter associated with the binuclear heme CuB site. The standard midpoint potentials of the cytochrome a587 heme centers are +210 and +270 mV, respectively
heme
-
the metal centers in the cytochrome aa3 from Sulfolobus consist of a low-spin heme a, a high-spin heme a3 and a CuB-type center. The heme a3 and the Cu, form a binuclear center
heme
-
the SoxABCD quinol oxidase complex probably contains four A-type hemes which are bound to SoxB and SoxC. The structure of these hemes is not identical to heme A. The Sulfolobus heme As has a 2-hydroxyethyl geranylgeranyl in position 2 of the porphyrin ring whereas heme A has the related farnesyl-containing side-chain
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu
Cu2+
Fe
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
the enzyme contains a total of seven metal redox centers. One of it, the blue copper protein sulfocyanin, functionally links two subcomplexes. One is a bb3-type terminal oxidase moiety containing CuA and CuB, whereas the other consists of a Rieske FeS-protein and a homolog to cytochrome b â in this case hosting two hemes AS. Based on a 1:1 stoichiometry, 1 mol complex contains 6 mol Fe and 4 mol Cu
copper
-
a type B heme-copper oxygen reductase. The binuclear Fea3âCu(B) center is the site of dioxygen chemistry and is involved in the proton translocation mechanism. The catalytic bimetallic Cu(B) center is probed in a number of different states using extended X-ray absorption fine structure (EXAFS) spectroscopy. The oxidized CuB center is four-coordinated with three histidine residues and one oxygen atom. No significant change in the protein structure in the vicinity of Cu(B) is observed upon reduction, apart from the release of the oxo ligand
copper
P39480; P98004; P39479; P39477
the enzyme contains one copper atom
copper
the recombinant subunit SoxH of the SoxM complex contains a correctly inserted binuclear Cu(A) cluster. In recombinant form, the metal interacts with cytochrome c as an artificial electron donor. The physiological electron donor is unknown, since Sulfolobus acidocaldarius does not contain any c-type cytochromes. The purple copper center of SoxM shows a pH dependency with a pKa at 6.4, suggesting protonation of the Cu-ligating histidines. Contains 1.3 Cu atoms per SoxH molecule
copper
-
the active respiratory terminal oxidase segment of Sulfolobus sp. strain 7 contains one non-CO-reactive b-type cytochrome (b562) and two different a-type cytochromes (a583 and aa3), in addition to one copper and a Rieske-type FeS cluster, which, as a whole, function as an active caldariellaquinol oxidase supercomplex
Cu
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
the enzyme contains a total of seven metal redox centers. One of it, the blue copper protein sulfocyanin, functionally links two subcomplexes. One is a bb3-type terminal oxidase moiety containing CuA and CuB, whereas the other consists of a Rieske FeS-protein and a homolog to cytochrome b â in this case hosting two hemes AS. Based on a 1:1 stoichiometry, 1 mol complex contains 6 mol Fe and 4 mol Cu
Cu2+
-
the metal centers in the cytochrome aa3 from Sulfolobus consist of a low-spin heme a, a high-spin heme a3 and a CuB-type center. The heme a3 and the Cu, form a binuclear center
Cu2+
-
the single subunit (38000-40000 Da) contains two copper ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
causes maximal inhibition of either the isolated enzyme, or the activity of the crude membrane extract by 63% with a half-maximal effect at 21 mM
ferrocytochrome c
-
0.002 mM, 50% inhibition of N,N,N',N'-tetramethyl-1,4-phenylenediamine-ascorbate dependent oxygen consumption
cyanide
P39480; P98004; P39479; P39477
2 mM, oxidation of caldariella quinol and N,N,N',N'-tetramethyl-1,4-phenylenediamine is completely inhibited
phosphate
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
inhibitory effect which at the pH-optimum and 50 mM phosphate concentration amounts to about 35%
additional information
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
benzoquinone, naphthoquinone and phenol derivatives do not influence the reactivity
-
additional information
-
no inhibition by myxothiazol, antimycin, funiculosin, 2-heptyl-4-hydroxyquinoline-N-oxide, 5-n-undecyl-6-hydroxy-2,7-dioxobenzothiazole and 3-(3,4-dichlorophenyl)-1,3-dimethylurea
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
N,N,N',N'-tetramethyl-1,4-phenylenediamine hydrochloride
-
pH 7.0, 40°C
0.026
caldariellaquinol
P39480; P98004; P39479; P39477
pH 6.5, 50°C, enzyme in liposomes (tetraether lipids)
0.036
caldariellaquinol
P39480; P98004; P39479; P39477
pH 6.5, 50°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside)
0.046
N,N,N',N'-tetramethyl-1,4-phenylenediamine
P39480; P98004; P39479; P39477
pH 6.5, 40°C, enzyme in liposomes (tetraether lipids)
0.067
N,N,N',N'-tetramethyl-1,4-phenylenediamine
P39480; P98004; P39479; P39477
pH 6.5, 40°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
239
caldariellaquinol
P39480; P98004; P39479; P39477
pH 6.5, 50°C, enzyme in liposomes (tetraether lipids)
393
caldariellaquinol
P39480; P98004; P39479; P39477
pH 6.5, 50°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside)
157
N,N,N',N'-tetramethyl-1,4-phenylenediamine
P39480; P98004; P39479; P39477
pH 6.5, 40°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside)
404
N,N,N',N'-tetramethyl-1,4-phenylenediamine
P39480; P98004; P39479; P39477
pH 6.5, 40°C, enzyme in liposomes (tetraether lipids)
additional information
additional information
-
menadiol and 2,3,5,6-tetrachlorobenzoquinol show turnover numbers of 30-40 e-/s. The highest activity of 100 e-/s can be obtained with N,N,N',N'-tetramethyl-1,4-phenylenediamine
-
additional information
additional information
-
two kinetic phases are observed. The first phase is attributed to binding of O2 to heme a3 and oxidation of both hemes forming the peroxy intermediate. The second phase is associated with proton uptake from solution and it is attributed to formation of the oxo-ferryl state, the final state in the absence of quinol. In the presence of bound caldariella quinol, heme a is re-reduced by caldariella quinol with a rate of 670/s, followed by transfer of the fourth electron to the binuclear center with a rate of 50/s
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9200
caldariellaquinol
P39480; P98004; P39479; P39477
pH 6.5, 50°C, enzyme in liposomes (tetraether lipids)
11000
caldariellaquinol
P39480; P98004; P39479; P39477
pH 6.5, 50°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside)
2300
N,N,N',N'-tetramethyl-1,4-phenylenediamine
P39480; P98004; P39479; P39477
pH 6.5, 40°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside)
8700
N,N,N',N'-tetramethyl-1,4-phenylenediamine
P39480; P98004; P39479; P39477
pH 6.5, 40°C, enzyme in liposomes (tetraether lipids)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36
-
pH 7.0, 40°C, oxidation of N,N,N',N'-tetramethyl-1,4-phenylenediamine hydrochloride
9.9
-
pH 6, 40°C, oxidation of N,N,N',N'-tetramethyl-1,4-phenylenediamine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P94117 (doxB, catalytic core), P94118 (doxC)
P94117; P94118
SwissProt
brenda
P94117 (doxB, catalytic core), P94118 (doxC). Subunits doxA and doxB later classified as EC 1.8.5.2, thiosulfate dehydrogenase (quinone)
P94117; P94118
SwissProt
brenda
P94117 (doxB, catalytic core), P94118 (doxC). Subunits doxA and doxB later classified as EC 1.8.5.2, thiosulfate dehydrogenase (quinone)
P94117; P94118
SwissProt
brenda
P39480 (soxA) and P98004 (soxB) and P39479 (soxA) and P39477 (Saci_2086)
P39480; P98004; P39479; P39477
SwissProt
brenda
P39480 (soxC) and P98004 (soxB) and P39479 (soxA) and P39477 (Saci_2086)
P39480; P98004; P39479; P39477
SwissProt
brenda
P39481 (soxM), Q97UN3 (soxG), Q53765 (soxE), Q53766 (soxD), Q59825 (soxH), Q53768 (soxI)
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
the enzyme may be involved in the electron pathway, it may be involved in regulatory adaptation to environmental stress
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). F2Z6G7_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
146
1
16336
TrEMBL
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QOXM_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
788
0
87082
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11000
-
x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE
149000
P94117; P94118
assuming a 1:1 stoichiometry of all encoded subunits, the Acidianus ambivalens aa3-type quinol oxidase represents a complex with a calculated molecular mass of 149000 Da. Subunits doxA and doxB later classified as EC 1.8.5.2, thiosulfate dehydrogenase (quinone)
18900
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x * 18900 (SoxA) + x * 58000 (SoxB) + x * 62600 (SoxC) + SoxD + ?. The SoxABCD quinol oxidase complex contains at least five different polypeptides. In addition to the major subunits SoxA, SoxB and SoxC, it has two small polypeptides. One of these is the translation product of a short open reading frame (called the soxD gene) at the end of the operon
19000
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x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE
280000
47000
-
x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE
570000
P39480; P98004; P39479; P39477
when membrane solubilization is carried out at low salt concentration, an oligomeric state of the oxidase is obtained
58000
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x * 18900 (SoxA) + x * 58000 (SoxB) + x * 62600 (SoxC) + SoxD + ?. The SoxABCD quinol oxidase complex contains at least five different polypeptides. In addition to the major subunits SoxA, SoxB and SoxC, it has two small polypeptides. One of these is the translation product of a short open reading frame (called the soxD gene) at the end of the operon
62600
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x * 18900 (SoxA) + x * 58000 (SoxB) + x * 62600 (SoxC) + SoxD + ?. The SoxABCD quinol oxidase complex contains at least five different polypeptides. In addition to the major subunits SoxA, SoxB and SoxC, it has two small polypeptides. One of these is the translation product of a short open reading frame (called the soxD gene) at the end of the operon
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
P94117; P94118
composed of at least five different subunits of 64900 Da, 38000 Da, 20400 Da, 18800 Da, and 7200 Da. Their genes are located in two different operons. While from both gene loci, a total of six genes are transcribed into mRNA, the pattern of polypeptides found in oxidase preparations comprises only four prominent protein bands on SDS-gels. The bands of 45000 Da, 40000 Da, 28000 Da, and 20000 Da can be assigned to proteins with calculated molecular masses of 38000 (DoxC), 64900 (DoxB), 18800 (DoxA), and 20400 (DoxD) Da, consistent with the frequent observation that membrane proteins display abnormal migration behavior upon denaturating SDS-PAGE. DoxB represents the catalytic core of the oxidase, exhibiting the typical consensus sequences for the heme- and copper-binding sites. Subunits doxA and doxB later classified as EC 1.8.5.2, thiosulfate dehydrogenase (quinone)
?
P94117; P94118
the doxD and doxA genes form a bicistronic operon in the Acidianus ambivalens genome, physically separated from the doxBCEF operon encoding the catalytic and the other subunits of the terminal quinol:oxygen oxidoreductase. Subunits with apparent molecular masses of 56000 Da (DoxB) and 61000 Da (DoxC) appear in the preparation of the terminal oxidase. Both enzymes 1. thiosulfate dehydrogenase (quinone) (EC 1.8.5.2, composed of the subunits DoxA and DoxD) and 2. caldariella quinol:dioxygen oxidoreductase (composed of the major subunits DoxB and DoxC and the minor subunit DoxE) form separate entities. The thiosulfate dehydrogenase (quinone) and the terminal oxidase might still form a loose aggregation in the membrane, transferring electrons rapidly either directly via the bound caldariella quinol molecule or indirectly via free caldariella quinol
?
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composed of at least five different subunits of 64900 Da, 38000 Da, 20400 Da, 18800 Da, and 7200 Da. Their genes are located in two different operons. While from both gene loci, a total of six genes are transcribed into mRNA, the pattern of polypeptides found in oxidase preparations comprises only four prominent protein bands on SDS-gels. The bands of 45000 Da, 40000 Da, 28000 Da, and 20000 Da can be assigned to proteins with calculated molecular masses of 38000 (DoxC), 64900 (DoxB), 18800 (DoxA), and 20400 (DoxD) Da, consistent with the frequent observation that membrane proteins display abnormal migration behavior upon denaturating SDS-PAGE. DoxB represents the catalytic core of the oxidase, exhibiting the typical consensus sequences for the heme- and copper-binding sites. Subunits doxA and doxB later classified as EC 1.8.5.2, thiosulfate dehydrogenase (quinone)
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?
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x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE
?
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x * 18900 (SoxA) + x * 58000 (SoxB) + x * 62600 (SoxC) + SoxD + ?. The SoxABCD quinol oxidase complex contains at least five different polypeptides. In addition to the major subunits SoxA, SoxB and SoxC, it has two small polypeptides. One of these is the translation product of a short open reading frame (called the soxD gene) at the end of the operon
additional information
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
6 polypeptide subunits: SoxM (87000 Da), SoxG (56000 Da), SoxE (21000 Da) , SoxF (26800 Da), SoxH (16300 Da), SoxI (16800 Da). Proposed structural organization of the supercomplex: therein the polypeptides SoxG, SoxF, and SoxE represent an assembly. Sulfocyanin (SoxE) has a typical membrane spanning N-terminal anchor sequence fixing it firmly to the complex
additional information
SoxM is the core component of a second terminal oxidase complex. It forms a complex with at least SoxC and a 30 kDa Rieske Fe-S protein, but neither with SoxA nor SoxB
additional information
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SoxM is the core component of a second terminal oxidase complex. It forms a complex with at least SoxC and a 30 kDa Rieske Fe-S protein, but neither with SoxA nor SoxB
additional information
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SoxE is a constituent of the SoxM terminal oxidase supercomplex whereas SoxH, the CuA containing subunit II, escapes from the membrane fraction during preparation
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
SoxM is probably a precursor form of subunits I and III
additional information
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SoxM is probably a precursor form of subunits I and III