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Information on EC 1.8.2.4 - dimethyl sulfide:cytochrome c2 reductase for references in articles please use BRENDA:EC1.8.2.4Word Map on EC 1.8.2.4
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The expected taxonomic range for this enzyme is: Rhodovulum sulfidophilum
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dimethyl sulfide:cytochrome c2 reductase
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dimethyl sulfide + 2 ferricytochrome c2 + H2O = dimethyl sulfoxide + 2 ferrocytochrome c2 + 2 H+
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oxidation
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dimethyl sulfide degradation III (oxidation)
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dimethyl sulfide:ferricytochrome-c2 oxidoreductase
The enzyme from the bacterium Rhodovulum sulfidophilum binds molybdopterin guanine dinucleotide, heme b and [4Fe-4S] clusters.
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dimethyl sulfide dehydrogenase
dimethyl sulphide dehydrogenase
dimethylsulfide: acceptor oxidoreductase
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DMS:ferricytochrome c2 oxidoreductase
Me2S:acceptor oxidoreductase
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-
DdhA
subunit
DdhB
subunit
DdhC
subunit
dimethyl sulfide dehydrogenase
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-
dimethyl sulfide dehydrogenase
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dimethyl sulphide dehydrogenase
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dimethyl sulphide dehydrogenase
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-
DMS dehydrogenase
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DMS DH
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DMS:ferricytochrome c2 oxidoreductase
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DMS:ferricytochrome c2 oxidoreductase
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subunit alpha (DdhA)
UniProt
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subunit beta (DdhB)
UniProt
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subunit gamma (DdhC)
UniProt
brenda
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-
-
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subunit alpha (DdhA)
UniProt
brenda
subunit beta (DdhB)
UniProt
brenda
subunit gamma (DdhC)
UniProt
brenda
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malfunction
the ddhA mutant is not able to grow photoautotrophically with dimethyl sulfide as electron donor, although photoheterotrophic growth is not impaired
malfunction
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the ddhA mutant is not able to grow photoautotrophically with dimethyl sulfide as electron donor, although photoheterotrophic growth is not impaired
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physiological function
dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate; dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate; dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate
physiological function
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dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate; dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate; dimethyl sulfide dehydrogenase is essential for photolithotrophic growth of Rhodovulum sulfidophilum on dimethyl sulfide but not for chemo-trophic growth on the same substrate
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dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
dimethyl sulfide + oxidized 2,6-dichlorophenolindophenol + H2O
dimethyl sulfoxide + reduced 2,6-dichlorophenolindophenol
dimethyl sulfoxide + reduced 2,6-dichloroindophenol
dimethyl sulfide + oxidized 2,6-dichloroindophenol + H2O
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-
?
dimethyl sulfoxide + reduced methyl viologen + H2O
dimethyl sulfide + oxidized methyl viologen
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2% activity compared to trimethylamine N-oxide
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-
?
lauryldimethylamine N-oxide + reduced methyl viologen + H2O
?
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69% activity compared to trimethylamine N-oxide
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-
?
trimethylamine N-oxide + reduced methyl viologen + H2O
?
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100% activity
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-
?
additional information
?
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no activity with chlorate and bromate
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dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism
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-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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DMS:ferrocytochrome oxidoreductase operates via a two-site ping-pong mechanism
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-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
-
?
dimethyl sulfide + oxidized 2,6-dichlorophenolindophenol + H2O
dimethyl sulfoxide + reduced 2,6-dichlorophenolindophenol
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-
-
?
dimethyl sulfide + oxidized 2,6-dichlorophenolindophenol + H2O
dimethyl sulfoxide + reduced 2,6-dichlorophenolindophenol
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-
-
?
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dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
Q8GPG1, Q8GPG3, Q8GPG4
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-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
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-
-
-
?
dimethyl sulfide + ferricytochrome c2 + H2O
dimethyl sulfoxide + ferrocytochrome c2
Q8GPG1, Q8GPG3, Q8GPG4
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?
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[3Fe-4S]-center
subunit DdhB binds one 3Fe-4S cluster
heme
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the cytochrome contains a b-type heme and a content of 0.65 mol protoheme per mol enzyme is determined
heme
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the enzyme contains a heme b cofactor
iron-sulfur centre
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iron-sulfur centre
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the enzyme contains five iron-sulfur clusters
molybdopterin
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molybdopterin
bis(molybdopterin guanine dinucleotide)Mo; bis(molybdopterin guanine dinucleotide)Mo; bis(molybdopterin guanine dinucleotide)Mo
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Fe
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the enzyme contains 3.5 mol Fe per mol enzyme
Iron
the enzyme contains 17 mol iron per mol enzyme; the enzyme contains 17 mol iron per mol enzyme; the enzyme contains 17 mol iron per mol enzyme
Molybdenum
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the enzyme contains 0.5 mol molybdenum per mol enzyme
Molybdenum
the enzyme contains 0.5 mol molybdenum per mol enzyme; the enzyme contains 0.5 mol molybdenum per mol enzyme; the enzyme contains 0.5 mol molybdenum per mol enzyme
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0.053
Dimethyl sulfide
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in 220 mM Tris-HCl pH 8.0, 22°C
0.021
ferricytochrome c2
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in 220 mM Tris-HCl pH 8.0, 22°C
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18.2
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crude extract, using reduced 2,6-dichloroindophenol as cosubstrate, in 50 mM Tris/HCI pH 8.0, temperature not specified in the publication
20.2
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after purification, using reduced 2,6-dichloroindophenol as cosubstrate, in 50 mM Tris/HCI pH 8.0, temperature not specified in the publication
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brenda
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brenda
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32000
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1 * 94000 + 1 * 38000 + 1 * 32000, SDS-PAGE
32000
1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; subunit DdhC
38000
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1 * 94000 + 1 * 38000 + 1 * 32000, SDS-PAGE
38000
1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; subunit DdhB
94000
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1 * 94000 + 1 * 38000 + 1 * 32000, SDS-PAGE
94000
1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; subunit DdhA
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heterotrimer
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1 * 94000 + 1 * 38000 + 1 * 32000, SDS-PAGE
heterotrimer
1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000
heterotrimer
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; 1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000; 1 * 94000 + 1 * 38000 + 1 * 32000
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ammonium sulfate precipitation, DEAE-Sepharose column chromatography, hydroxyapatite column chromatography, and Sephacryl S-200 gel filtration
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ammonium sulfate precipitation, SP-Sepharose column chromatography, gel filtration
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Poros 20HQ Strong anion exchange column chromatography and gel filtration; Poros 20HQ Strong anion exchange column chromatography and gel filtration; Poros 20HQ Strong anion exchange column chromatography and gel filtration
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DDHA_RHOSU
910
102309
Swiss-Prot
A0A2T9P9K4_SALTH
1020
110993
TrEMBL
A0A2X4QVE2_SALCE
1020
110883
TrEMBL
A0A143X7X2_9ACTN
815
89497
TrEMBL
A0A181Y2Z6_KLEOX
962
107553
TrEMBL
A0A2X2MN52_SERMA
1023
110237
TrEMBL
A0A2X4T833_SALSE
1020
110977
TrEMBL
A0A2X1TWZ0_MORMO
1029
111623
TrEMBL
A0A2X4TCN4_SALCE
1020
110889
TrEMBL
A0A2X2DQW5_PRORE
1024
112043
TrEMBL
A0A2X1XQ73_PROMI
1027
112139
TrEMBL
A0A239SPL4_9BURK
1153
125427
TrEMBL
A0A0U1K8Q7_YERMO
1028
111724
TrEMBL
A0A1M8M093_9MYCO
1128
122224
TrEMBL
A0A173V2M5_EUBRA
Eubacterium ramulus
880
99714
TrEMBL
A0A2X2Q073_9ENTR
1023
110759
TrEMBL
A0A2I5HHC6_SALDZ
Salmonella diarizonae
1020
110850
TrEMBL
A0A2X4M525_SALCE
1020
110800
TrEMBL
A0A2X4NGQ5_AERCA
1035
111957
TrEMBL
A0A156FBP7_ENTCL
1021
110928
TrEMBL
A0A2X2BFJ2_PROMI
650
70714
TrEMBL
A0A1J5RYR3_9ZZZZ
914
100551
TrEMBL
A0A2X4VLG9_PASMD
1029
113126
TrEMBL
Q8Z6K5_SALTI
1020
111034
TrEMBL
A0A143X6Z2_9ACTN
909
101893
TrEMBL
A0A2X4QJJ2_SALET
1020
110968
TrEMBL
A0A2X5BRD2_SALET
659
71562
TrEMBL
A0A2X8A9P1_ECOLX
1021
110952
TrEMBL
S0G7M7_9DELT
814
91966
TrEMBL
A0A2X4XHK8_SALCE
1020
110808
TrEMBL
A0A2X4SC65_SALET
1020
111005
TrEMBL
A0A2X4YGP1_SALET
1020
110945
TrEMBL
A0A2X1XFK2_9PAST
1029
113018
TrEMBL
A0A143X7Q0_9ACTN
941
104305
TrEMBL
A0A2X1H7M9_BURCE
978
108793
TrEMBL
A0A2X2NNE9_VIBAL
1030
113116
TrEMBL
A0A2X4Q4E1_SALET
1020
111035
TrEMBL
A0A2Y0LHS6_ECOLX
1021
110878
TrEMBL
A0A0U1F993_SALTM
1020
110993
TrEMBL
A0A2X4ULP6_SALET
1020
111005
TrEMBL
A0A2X5F4I4_SALET
242
26592
TrEMBL
A0A259U9M8_9FIRM
894
100145
TrEMBL
A0A2X5AV41_SALET
619
67095
TrEMBL
A0A1C6B1U6_9FIRM
uncultured Roseburia sp
892
100666
TrEMBL
A0A168EBM4_KLEOX
1021
110394
TrEMBL
A0A168YY84_KLEOX
1023
110508
TrEMBL
A0A0T7RNC4_SALET
1020
110981
TrEMBL
A0A2X4MBJ0_SALET
1020
111024
TrEMBL
A0A2X4JR44_9GAMM
1024
111957
TrEMBL
A0A2X4XW63_SALIN
1020
110993
TrEMBL
A0A2X4W7A9_SALCE
1020
110897
TrEMBL
A0A0F1Q3Z7_ENTCL
1146
127426
TrEMBL
DDHB_RHOSU
325
37026
Swiss-Prot
DDHC_RHOSU
265
29499
Swiss-Prot
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Hanlon, S.; Toh, T.; Solomon, P.; Holt, R.; McEwan, A.
Dimethylsulfide: acceptor oxidoreductase from Rhodobacter sulfidophilus - The purified enzyme contains b-type haem and a pterin molybdenum cofactor
Eur. J. Biochem.
239
391-396
1996
Rhodovulum sulfidophilum
brenda
Creevey, N.; McEwan, A.; Bernhardt, P.
A mechanistic and electrochemical study of the interaction between dimethyl sulfide dehydrogenase and its electron transfer partner cytochrome c2
J. Biol. Inorg. Chem.
13
1231-1238
2008
Rhodovulum sulfidophilum, Rhodovulum sulfidophilum SH1
brenda
McDevitt, C.; Hugenholtz, P.; Hanson, G.; McEwan, A.
Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: Its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes
Mol. Microbiol.
44
1575-1587
2002
Rhodovulum sulfidophilum (Q8GPG1), Rhodovulum sulfidophilum (Q8GPG3), Rhodovulum sulfidophilum (Q8GPG4), Rhodovulum sulfidophilum, Rhodovulum sulfidophilum SH1 (Q8GPG1), Rhodovulum sulfidophilum SH1 (Q8GPG3), Rhodovulum sulfidophilum SH1 (Q8GPG4)
brenda
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