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2 caldariellaquinol + O2 + n H+[side 1]
2 caldariellaquinone + 2 H2O + n H+[side 2]
2,3,5,6-tetrachlorobenzoquinol + oxidized dithiothreitol
?
-
-
-
-
?
4 ferrocytochrome c + O2 + 4 H+
4 ferricytochrome c + 2 H2O
caldariella quinol + O2 + n H+/in
caldariella quinone + H2O + n H+/out
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
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
-
-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine hydrochloride + O2
?
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
-
-
-
-
?
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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239 - 393
caldariellaquinol
1.5
ferrocytochrome c
-
pH 7.5, 40°C
66.9 - 404
N,N,N',N'-tetramethyl-1,4-phenylenediamine
additional information
additional information
-
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)
66.9
N,N,N',N'-tetramethyl-1,4-phenylenediamine
-
pH 7.5, 25°C
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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100000 - 104000
-
gel filtration
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
-
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
-
x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE
20000
-
x * 40000 + x * 27000 + x * 20000, SDS-PAGE
224000
P39481; Q97UN3; Q53765; Q53766; Q59825; Q53768
gel filtration
27000
-
x * 40000 + x * 27000 + x * 20000, SDS-PAGE
40000
-
x * 40000 + x * 27000 + x * 20000, SDS-PAGE
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
-
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
-
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
87082
x * 87082, calulated from sequence
280000
P39480; P98004; P39479; P39477
gel filtration
280000
-
detergent-SoxABCD protein complex, gel filtration
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?
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
?
-
x * 40000 + x * 27000 + x * 20000, SDS-PAGE
?
-
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)
-
?
-
x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE
?
-
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
?
x * 87082, calulated from sequence
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
-
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
-
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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Anemuller, S.; Schäfer, G.
Cytochrome aa3 from Sulfolobus acidocaldarius. A single-subunit, quinol-oxidizing archaebacterial terminal oxidase
Eur. J. Biochem.
191
297-305
1990
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
brenda
Muller, F.H.; Bandeiras, T.M.; Urich, T.; Teixeira, M.; Gomes, C.M.; Kletzin, A.
Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase
Mol. Microbiol.
53
1147-1160
2004
Acidianus ambivalens (P94117 and P94118), Acidianus ambivalens
brenda
Anemüller, S.; Bill, E.; Schäfer, G.; Trautwein, A.X.; Teixeira, M.
EPR studies of cytochrome aa3 from Sulfolobus acidocaldarius. Evidence for a binuclear center in archaebacterial terminal oxidase.
Eur. J. Biochem.
210
133-138
1992
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
brenda
Gleissner, M.; Elferink, M.G.; Driessen, A.J.; Konings, W.N.; Anemüller, S.; Schäfer, G.
Generation of proton-motive force by an archaeal terminal quinol oxidase from Sulfolobus acidocaldarius
Eur. J. Biochem.
224
983-990
1994
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639
brenda
Iwasaki, T.; Wakagi, T.; Isogai, Y.; Iizuka, T.; Oshima, T.
Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. strain 7 II. Characterization of the archaeal terminal oxidase subcomplexes and implication for the intramolecular electron transfer
J. Biol. Chem.
270
30893-30901
1995
Sulfolobus sp., Sulfolobus sp. 7
brenda
Ishikawa, R.; Ishido, Y.; Tachikawa, A.; Kawasaki, H.; Matsuzawa, H.; Wakagi, T.
Aeropyrum pernix K1, a strictly aerobic and hyperthermophilic archaeon, has two terminal oxidases, cytochrome ba3 and cytochrome aa3
Arch. Microbiol.
179
42-49
2002
Aeropyrum pernix
brenda
Gilderson, G.; Aagaard, A.; Gomes, C.M.; Adelroth, P.; Teixeira, M.; Brzezinski, P.
Kinetics of electron and proton transfer during O(2) reduction in cytochrome aa(3) from A. ambivalens: an enzyme lacking Glu(I-286)
Biochim. Biophys. Acta
1503
261-270
2001
Acidianus ambivalens, Acidianus ambivalens DSM 3772
brenda
Komorowski, L.; Verheyen, W.; Schäfer, G.
The archaeal respiratory supercomplex SoxM from Sulfolobus acidocaldarius combines features of quinole and cytochrome c oxidases
Biol. Chem.
383
1791-1799
2002
Sulfolobus acidocaldarius (P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768)
brenda
Lübben, M.; Kolmerer, B.; Saraste, M.
An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes
EMBO J.
11
805-812
1992
Sulfolobus acidocaldarius (P39480 and P98004 and P39479 and P39477)
brenda
Luebben, M.; Arnaud, S.; Castresana, J.; Warne, A.; Albracht, S.P.; Saraste, M.
A second terminal oxidase in Sulfolobus acidocaldarius
Eur. J. Biochem.
224
151-159
1994
Sulfolobus acidocaldarius (P39481), Sulfolobus acidocaldarius
brenda
Giuffre, A.; Gomes, C.M.; Antonini, G.; D'Itri, E.; Teixeira, M.; Brunori, M.
Functional properties of the quinol oxidase from Acidianus ambivalens and the possible catalytic role of its electron donor. Studies on the membrane-integrated and purified enzyme
Eur. J. Biochem.
250
383-388
1997
Acidianus ambivalens
brenda
Anemüller, S.; Schmidt, C.L.; Pacheco, I.; Schäfer, G.; Teixeira, M.
A cytochrome aa3-type quinol oxidase from Desulfurolobus ambivalens, the most acidophilic archaeon
FEMS Microbiol. Lett.
117
275-280
1994
Acidianus ambivalens
-
brenda
Purschke, W.G.; Schmidt, C.L.; Petersen, A.; Schäfer, G.
The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization
J. Bacteriol.
179
1344-1353
1997
Acidianus ambivalens (P94117 and P94118), Acidianus ambivalens, Acidianus ambivalens DSM 3772 (P94117 and P94118)
brenda
Komorowski, L.; Anemüller, S.; Schäfer, G.
First expression and characterization of a recombinant CuA-containing subunit II from an archaeal terminal oxidase complex
J. Bioenerg. Biomembr.
33
27-34
2001
Sulfolobus acidocaldarius (F2Z6G7)
brenda
Giuffre, A.; Antonini, G.; Brunori, M.; D'Itri, E.; Malatesta, F.; Nicoletti, F.; Anemueller, S.; Gleissner, M.; Schaefer, G.
Sulfolobus acidocaldarius terminal oxidase. A kinetic investigation and its structural interpretation
J. Biol. Chem.
269
31006-31011
1994
Sulfolobus acidocaldarius
brenda
Gleissner, M.; Kaiser, U.; Antonopoulos, E.; Schäfer, G.
The archaeal SoxABCD complex is a proton pump in Sulfolobus acidocaldarius
J. Biol. Chem.
272
8417-8426
1997
Sulfolobus acidocaldarius (P39480 and P98004 and P39479 and P39477), Sulfolobus acidocaldarius
brenda
Bandeiras, T.M.; Pereira, M.M.; Teixeira, M.; Moenne-Loccoz, P.; Blackburn, N.J.
Structure and coordination of CuB in the Acidianus ambivalens aa3 quinol oxidase heme-copper center
J. Biol. Inorg. Chem.
10
625-635
2005
Acidianus ambivalens
brenda
Luebben, M.; Warne, A.; Albracht, S.P.; Saraste, M.
The purified SoxABCD quinol oxidase complex of Sulfolobus acidocaldarius contains a novel haem
Mol. Microbiol.
13
327-335
1994
Sulfolobus acidocaldarius
brenda
Das, T.K.; Gomes, C.M.; Teixeira, M.; Rousseau, D.L.
Redox-linked transient deprotonation at the binuclear site in the aa(3)-type quinol oxidase from Acidianus ambivalens: implications for proton translocation
Proc. Natl. Acad. Sci. USA
96
9591-9596
1999
Acidianus ambivalens
brenda
Iwasaki, T.; Matsuura, K.; Oshima, T.
Resolution of the aerobic respiratory system of the thermoacidophilic archaeon, Sulfolobus sp. strain 7. I. The archaeal terminal oxidase supercomplex is a functional fusion of respiratory complexes III and IV with no c-type cytochromes
J. Biol. Chem.
270
30881-30892
1995
Sulfolobus sp., Sulfolobus sp. 7
brenda
Komorowski, L.; Schäfer, G.
Sulfocyanin and subunit II, two copper proteins with novel features, provide new insight into the archaeal SoxM oxidase supercomplex
FEBS Lett.
487
351-355
2001
Sulfolobus acidocaldarius
brenda
Gomes, C.M.; Backgren, C.; Teixeira, M.; Puustinen, A.; Verkhovskaya, M.L.; Wikström, M.; Verkhovsky, M.I.
Heme-copper oxidases with modified D- and K-pathways are yet efficient proton pumps
FEBS Lett.
497
159-164
2001
Acidianus ambivalens
brenda
Castelle, C.J.; Roger, M.; Bauzan, M.; Brugna, M.; Lignon, S.; Nimtz, M.; Golyshina, O.V.; Giudici-Orticoni, M.T.; Guiral, M.
The aerobic respiratory chain of the acidophilic archaeon Ferroplasma acidiphilum A membrane-bound complex oxidizing ferrous iron
Biochim. Biophys. Acta
1847
717-728
2015
Ferroplasma acidiphilum
brenda