1.8.5.3: respiratory dimethylsulfoxide reductase
This is an abbreviated version!
For detailed information about respiratory dimethylsulfoxide reductase, go to the full flat file.
Word Map on EC 1.8.5.3
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1.8.5.3
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rhodobacter
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sphaeroides
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molybdoenzyme
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molybdopterin
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capsulatus
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dithiolene
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pyranopterins
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narghi
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tord
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bismolybdopterin
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mo-containing
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high-g
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menaquinol
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wiv
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frdabcd
- 1.8.5.3
- rhodobacter
- sphaeroides
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molybdoenzyme
- molybdopterin
- capsulatus
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dithiolene
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pyranopterins
- narghi
- tord
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bismolybdopterin
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mo-containing
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high-g
- menaquinol
- wiv
- frdabcd
Reaction
Synonyms
dimethyl sulfoxid reductase, dimethyl sulfoxide reductase, dimethyl sulfoxide/trimethylamine N-oxide reductase, dimethyl sulfoxie reductase, dimethylsulfoxide reductase, dms, DmsA, DmsABC, DmsABC sulfoxide reductase, DmsC, DMSO reductase, DMSOR, dorA, More, respiratory dimethyl sulfoxide reductase
ECTree
1.8.5.3 respiratory dimethylsulfoxide reductaseAdvanced search results
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results (Engineering
Engineering on EC 1.8.5.3 - respiratory dimethylsulfoxide reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Y114A
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mutation in direction of the active site of trimethylamine-N-oxide reduxtase. Mutation results in decreased specificity for S-oxides and an increased specificity for trimethylamine-N-oxide
Y114F
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mutation in direction of the active site of tiomethylamine-N-oxide reduxtase. Mutation results in decreased specificity for S-oxides and an increased specificity for trimethylamine-N-oxide
A178Q
A181T
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mutation in subunit DmsA. About 300% of wild-type catalytic efficiency
C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. The midpoint potential of FS4[3Fe-4S] is insensitive to inhibitor 2-n-heptyl-4-hydroxyquinoline N-oxide as well as to changes in pH from 5 to 7
C38S
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the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is significantly modified in DmsA-C38S mutant that contains a [3Fe-4S] cluster in DmsA. In ferricyanide-oxidized glycerol-inhibited DmsAC38SBC, there is no detectable interaction between the oxidized [3Fe-4S] cluster and the molybdo bis(molybdopterin guanine dinucleotide) cofactor
C59S
mutantion renders enzyme maturation sensitive to molybdenum cofactor availability. Residue C59 is a ligand to the FS0 [4Fe-4S] cluster. In the presence of trace amounts of molybdate, the C59S variant assembles normally to the cytoplasmic membrane and supports respiratory growth on DMSO, although the ground state of FS0 as determined by EPR is converted from high-spin, S = 3/2, to low-spin, S = 1/2. In the presence of the molybdenum antagonist tungstate, wild-type enzyme lacks molybdo-bis(pyranopterin guanine dinucleotide), but is translocated via the Tat translocon and assembles on the periplasmic side of the membrane as an apoenzyme. The C59S variant cannot overcome the dual insults of amino acid substitution plus lack of molybdo-bis(pyranopterin guanine dinucleotide) , leading to degradation of the DmsABC subunits
D95A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D95K/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D97A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
DELTAN21
mutant prevents molybdo-bis(pyranopterin guanine dinucleotide) binding and results in a degenerate [3Fe-4S] clusterform being assembled
G167N
G190D
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mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
G190V
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mutation in subunit DmsA. About 180% of wild-type catalytic efficiency
H106A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106E/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106I/C102S 2
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H65R
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mutation in subunit DmsC. Mutant blocks binding of the menaquinol analogue 2-n-heptyl-4-hydroxyquinoline-N-oxide to the protein
H85F/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H85T/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
K77A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
M147I
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mutation in subunit DmsA. About 65% of wild-type catalytic efficiency
M147L
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mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
P80A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Q179I
R103A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
R149C
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mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
R217Q
R61K
molybdo-bis(pyranopterin guanine dinucleotide) content is 90% of wild-type, decrease in specific activity
R77S
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DmsA-R77S mutant, the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is eliminated
S176A/C102S
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double mutant DmsA-S176A and DmsB-C102S, contains an engineered [3Fe-4S] cluster in DmsB, no significant paramagnetic interaction is detected between the oxidized [3Fe-4S] cluster and the Mo(V)
T148S
V20Y/DELTAN21/P27G
introduction of a type I Cys group, mutations eliminate both molybdo-bis(pyranopterin guanine dinucleotide) binding and detection of a FSo cluster by EPR
V20Y/DELTAN21/P27G/R61K
addtion of mutation R61K to mutant V20Y/DELTAN21/P27G partially rescues molybdo-bis(pyranopterin guanine dinucleotide) insertion
W191G
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mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
W357C
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mutation in subunit DmsA. About 100% of wild-type catalytic efficiency
W357F
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mutation in subunit DmsA. About 40% of wild-type catalytic efficiency
W357Y
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mutation in subunit DmsA. About 60% of wild-type catalytic efficiency
Y104A/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104D/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 150 mV. The midpoint potential of FS4 increases in the presence of 2-n-heptyl-4-hydroxyquinoline N-oxide and decreasing pH
Y104D/H106F/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104E/C102S
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mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 145 mV
W116F
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residue W116 forms a hydrogen bond with a single oxo ligand bound to the molybdenum ion. Mutation of this residue to phenylalanine affects the UV/visible spectrum of the purified MoVI form of dimethylsulfoxide reductase resulting in the loss of the characteristic transition at 720 nm
additional information
A178Q
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mutation in subunit DmsA. About 1200% of wild-type catalytic efficiency
A178Q
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mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
G167N
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mutation in subunit DmsA. About 20% of wild-type catalytic efficiency
G167N
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mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
Q179I
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mutation in subunit DmsA. About 500% of wild-type catalytic efficiency
Q179I
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mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
R217Q
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mutation in subunit DmsA. About 2.7% of wild-type catalytic efficiency
R217Q
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mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
T148S
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mutation in subunit DmsA. About 150% of wild-type catalytic efficiency
T148S
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mutation in subunit DmsA. Mutant shows altered kinetic parameters for pyridine N-oxide and dimethylsulfoxide, with Km and kcat decreasing and increasing approximately fourfold,respectively
additional information
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construction of a number of strains lacking portions of the chromosomal dmsABC operon. The mutant strains fail to grow anaerobically on glycerol minimal medium with dimethyl sulfoxide as the sole terminal oxidant but exhibit normal growth with nitrate, fumarate, and trimethylamine N-oxide. In vivo complementation of the mutant with plasmids carrying various dms genes, singly or in combination, reveal that the expression of all three subunits is essential to restore anaerobic growth. Expression of the DmsAB subunits without DmsC results in accumulation of the catalytically active dimer in the cytoplasm. The dimer is thermolabile and catalyzes the reduction of various substrates in the presence of artificial electron donors. Dimethylnaphthoquinol is oxidized only by the holoenzyme. Results suggest that the membrane-intrinsic subunit is necessary for anchoring, stability, and electron transport. The C-terminal region of DmsB appears to interact with the anchor peptide and facilitates the membrane assembly of the catalytic dimer
additional information
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overexpression of a subunit DmsC-dystrophin-specific amino acid sequence construct is toxic to Escherichia coli cells. Toxicity may be overcome by expression in a F0F1-ATPase mutant strain. Overexpression in COS-1 or McA-RH777 cells is not toxic and protein is localized to the endoplasmic reticulum
additional information
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molybdopterin enzyme periplasmic nitrate reductase (NapA, EC 1.9.6.1) is utilized as a vehicle to understand the substrate preference and delineate the kinetic underpinning of the differences imposed by exchanging the molybdenum ligands. The Mo-coordinating residue mutant C176D of NapA (EC 1.9.6.1), constructed by site-directed mutagenesis, is active with DMSO (and artificial cosubstrate methyl viologen), while the wild-type NapA is not. Kinetic consequences of the exchange of the endogenous ligand to molybdenum with other ligands within the cofactor of DMSO reductase family enzymes, overview. The C176D NapA variant shows attenuated nitrate reductase activity with a kcat 17times lower than the native NapA enzyme and a Km for nitrate that is 1.5times higher than the Km for nitrate reduction by the C176S NapA variant. Proposed interaction of the Asp ligand with bound DMSO compared to a Cys ligand at the active site in NapA variants
additional information
a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
additional information
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a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
additional information
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a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
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additional information
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a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
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additional information
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a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
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additional information
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a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
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additional information
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to investigate whether the subunits from these two DMSO reductases are interchangeable, two unmarked double in-frame DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 deletion mutants are constructed. Physiological assays demonstrate that the two double mutants lose the ability to utilize DMSO for anaerobic growth under different conditions. Moreover, transcriptional analyses reveal that deletion of the individual gene does not eliminate the expression of other genes within the same gene cluster. The loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants can be rescued by introduction of dmsA1 and dmsA6, respectively. Two complemented strains (the DELTAdmsA1/DELTAdmsB6-dmsA1-C and DELTAdmsA6/DELTAdmsB1-dmsA6-C strains [where -C refers to complementation]) are generated. The introduction of either dmsA1 into the DELTAdmsA1/DELTAdmsB6 mutant or dmsA6 into the DELTAdmsA6/DELTAdmsB1 mutant partially restores the ability of these double mutants to utilize DMSO for anaerobic growth. Growth curves of wild-type and mutant WP3 strains with DMSO as the sole electron acceptor, overview. Mutational analysis of subcellular localization of isozymes
additional information
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to investigate whether the subunits from these two DMSO reductases are interchangeable, two unmarked double in-frame DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 deletion mutants are constructed. Physiological assays demonstrate that the two double mutants lose the ability to utilize DMSO for anaerobic growth under different conditions. Moreover, transcriptional analyses reveal that deletion of the individual gene does not eliminate the expression of other genes within the same gene cluster. The loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants can be rescued by introduction of dmsA1 and dmsA6, respectively. Two complemented strains (the DELTAdmsA1/DELTAdmsB6-dmsA1-C and DELTAdmsA6/DELTAdmsB1-dmsA6-C strains [where -C refers to complementation]) are generated. The introduction of either dmsA1 into the DELTAdmsA1/DELTAdmsB6 mutant or dmsA6 into the DELTAdmsA6/DELTAdmsB1 mutant partially restores the ability of these double mutants to utilize DMSO for anaerobic growth. Growth curves of wild-type and mutant WP3 strains with DMSO as the sole electron acceptor, overview. Mutational analysis of subcellular localization of isozymes
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