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
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General Information
General Information on EC 1.8.5.3 - respiratory dimethylsulfoxide reductase
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evolution
malfunction
metabolism
physiological function
additional information
dimethyl sulfoxide reductase (DMSOR) represents the canonical member of the DMSOR family of prokaryotic pyranopterin molybdenum enzymes. DMSOR family enzymes have been classified by type, with type II/III enzymes being characterized by [(PDT)2MoVIO(OSer/Asp)]- oxidized active sites that possess N- and S-oxide reductase activity. Type III Rhodobacter capsulatus DMSOR catalyzes the reduction of dimethyl sulfoxide to dimethyl sulfide (DMS) as part of the global sulfur cycle
evolution
dimethyl sulfoxide reductase (DMSOR) represents the canonical member of the DMSOR family of prokaryotic pyranopterin molybdenum enzymes. DMSOR family enzymes have been classified by type, with type II/III enzymes being characterized by [(PDT)2MoVIO(OSer/Asp)]- oxidized active sites that possess N- and S-oxide reductase activity. Type III Rhodobacter sphaeroides DMSOR catalyzes the reduction of dimethyl sulfoxide to dimethyl sulfide (DMS) as part of the global sulfur cycle
evolution
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respiratory enzyme members of the DMSOR family such as nitrate reductase (NR, EC 1.9.6.1), dimethyl sulfoxide reductase (DMSOR, EC 1.8.5.3), trimethylamine N-oxide reductase (TMAOR, EC 1.7.2.3), and formate dehydrogenase (FDH) contribute to this broad diversity. The DMSOR family of enzymes has diverse active sites that vary in the first coordination sphere of the molybdenum center. Many enzymes in the DMSOR family use oxygen atom transfer (OAT) reactions for substrate transformation, e.g. periplasmic nitrate reductase (Nap) and respiratory nitrate reductase (Nar) reduce nitrate to nitrite, TMAOR reduces TMAO to TMA, and DMSOR reduces DMSO to dimethyl sulfide (DMS). Enzymes that catalyze the same reaction, such as Nap and Nar, have different molybdenum coordination spheres. In NapA, molybdenum is coordinated by a cysteine residue in the 5th position and an oxo or a sulfido group in the 6th
evolution
the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea. Dual activity has been described in DMSO reductases, as in the case of the Escherichia coli DMSO reductase that can reduce TMAO and other. In contrast, no DMSO reductase activity has been found in biochemically characterized TMAO reductases (EC 1.7.2.3)
evolution
the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea
evolution
the enzyme belongs to the dimethyl sulfoxide (DMSO) reductase family. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The DMSO reductase family enzymes are divided into three classes (Types I, II, and III) that are distinguished from each other by their active site structure and the nature of the donor ligand that is provided by the polypeptide. DMSO reductase family enzymes are quite diverse and not all of the enzymes in this family adhere to this general classification scheme. DMSO reductases are type III enzymes and a combination of EXAFS and high resolution X-ray crystallography shows that the oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry
evolution
the enzyme belongs to the dimethyl sulfoxide (DMSO) reductase family. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The DMSO reductase family enzymes are divided into three classes (Types I, II, and III) that are distinguished from each other by their active site structure and the nature of the donor ligand that is provided by the polypeptide. DMSO reductase family enzymes are quite diverse and not all of the enzymes in this family adhere to this general classification scheme. DMSO reductases are type III enzymes and a combination of EXAFS and high resolution X-ray crystallography shows that the oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry
evolution
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type VI and type I DMSO reductases are closely evolutionarily related. But both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship. Classification and phylogenetic analysis of DMSO respiratory subsystems in Shewanella species, overview
evolution
ubiquitous in Archaea and Bacteria, mononuclear molybdoenzymes of the dimethyl sulfoxide reductase (DMSOR) family are believed to have been core components of the first anaerobic respiratory chains, and thus present at life's origins. The family, which has been defined by the presence of a mononuclear molybdopterin or tungstopterin bis(pyranopterin guanine dinucleotide) (Mo/W-bisPGD) cofactor, is named after DMSO reductases, the first members of the family to be well-characterized. Phylogenetic analysis of DMSOR family clades and members, detailed overview. The enzyme belongs to a clade of DMSOR members that include the respiratory dimethyl sulfoxide reductase (DmsA), respiratory nitrate reductase (NarG), PsrA/PhsA/SrrA, ArxA/ArrA, and TtrA/SrdA/archaeal arsenate reductase lineages that interact with the membrane quinone pool during anaerobic respiration using the canonical subunits. The association of DMSOR members with characteristic electron transfer and membrane anchor subunits arose once early in the evolution of DSMORs and co-evolved with these representatives through multiple diversification events
evolution
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type VI and type I DMSO reductases are closely evolutionarily related. But both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship. Classification and phylogenetic analysis of DMSO respiratory subsystems in Shewanella species, overview
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evolution
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the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea. Dual activity has been described in DMSO reductases, as in the case of the Escherichia coli DMSO reductase that can reduce TMAO and other. In contrast, no DMSO reductase activity has been found in biochemically characterized TMAO reductases (EC 1.7.2.3)
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evolution
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the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea
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evolution
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the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea
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loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
malfunction
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loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants, which can be rescued by introduction of dmsA1 and dmsA6, respectively. The deficiencies of DMSO-dependent growth in DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants are attributable to the inability to form functional DMSO reductases rather than to the silencing of the expression of both dms gene clusters. In other words, functional compensation did not occur between DmsA1 and DmsA6 or between DmsB1 and DmsB6
malfunction
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loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants, which can be rescued by introduction of dmsA1 and dmsA6, respectively. The deficiencies of DMSO-dependent growth in DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants are attributable to the inability to form functional DMSO reductases rather than to the silencing of the expression of both dms gene clusters. In other words, functional compensation did not occur between DmsA1 and DmsA6 or between DmsB1 and DmsB6
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malfunction
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loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
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malfunction
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loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
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malfunction
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loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
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malfunction
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loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
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two functional DMSO respiratory subsystems are essential for maximum growth of strain WP3 under in situ conditions (4C/20 MPa). A core electron transport model of DMSO reduction in the deep-sea bacterium Shewanella piezotolerans strain WP3 is proposed based on genetic and physiological data, overview. The results collectively suggest that the possession of two sets of DMSO reductases with distinct subcellular localizations may be an adaptive strategy for WP3 to achieve maximum DMSO utilization in deep-sea environments. CymA serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE- and DmsF-independent manner. DmsE passes electrons to DmsA1 for DMSO reduction. Type VI DMSO reductase accepts electrons from CymA in a DmsE-independent manner, while type I DMSO reductase is strongly dependent on DmsE for electron transfer. DmsF, an integral outer membrane beta-barrel protein, facilitates electron transfer by forming a pore-like structure through the outer membrane to mediate direct interaction between the extracellular DMSO reductase and DmsE
metabolism
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two functional DMSO respiratory subsystems are essential for maximum growth of strain WP3 under in situ conditions (4C/20 MPa). A core electron transport model of DMSO reduction in the deep-sea bacterium Shewanella piezotolerans strain WP3 is proposed based on genetic and physiological data, overview. The results collectively suggest that the possession of two sets of DMSO reductases with distinct subcellular localizations may be an adaptive strategy for WP3 to achieve maximum DMSO utilization in deep-sea environments. CymA serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE- and DmsF-independent manner. DmsE passes electrons to DmsA1 for DMSO reduction. Type VI DMSO reductase accepts electrons from CymA in a DmsE-independent manner, while type I DMSO reductase is strongly dependent on DmsE for electron transfer. DmsF, an integral outer membrane beta-barrel protein, facilitates electron transfer by forming a pore-like structure through the outer membrane to mediate direct interaction between the extracellular DMSO reductase and DmsE
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anaerobic growth on sulfoxides is solely due to DmsABC expression
physiological function
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deletion mutant of catayltic subunit DmsA is attenuated in acute disease in an aerosol infection model
physiological function
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deletion mutants lacking dimethysulfoxide reductase retain the ability to use trimethylamine N-oxide as an electron acceptor and the trimethylamine N-oxid reductase activity is unaltered
physiological function
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more than 50% of chlorate-resistant mutants isolated are defective in the biosynthesis of the molybdenum cofactor and all of these mutants accumulate the precursor form of the enzyme. About 45% of the mutants contain the same level of molybdenum cofactor as the parent strain and exhibit normal levels of DMSO reductase and nitrate reductase activities when chlorate is absent from the medium, but the activities of these enzymes are depressed when chlorate is present. Much of the accumulated precursor form of the enzyme in a molybdenum cofactor-deficient mutant is bound to the cytoplasmic membrane and is sensitive to treatment with proteinase K from the periplasmic side of the membrane. Results suggest that the molybdenum cofactor is necessary for proteolytic processing of the precursor to the mature enzyme on the periplasmic side of the membrane, whereas binding of the precursor to the membrane and translocation across it can occur in the absence of the cofactor
physiological function
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mutants of Escherichia coli blocked in menaquinone biosynthesis, menB, menC, and menD, are unable to grow with DMSO as an electron acceptor, even though the terminal reductase is present in these mutants. Both growth and DMSO reduction can be restored in these mutants by growth in the presence of the menaquinone intermediates, o-succinylbenzoate and 1,4-dihydroxy-2-naphthoate, depending on the metabolic block of the mutant
physiological function
bacterial DMSO reductase and trimethylamine-N-oxide reductase (TMAO reductase) are of increasing environmental importance since they catalyze the oxidation of marine osmolytes and facilitate cloud formation and albedo
physiological function
bacterial DMSO reductase and trimethylamine-N-oxide reductase (TMAO reductase) are of increasing environmental importance since they catalyze the oxidation of marine osmolytes and facilitate cloud formation and albedo
physiological function
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dimethyl sulfoxide (DMSO) is an environmentally significant compound due to the potential role that it plays in the biogeochemical cycle of the climatically active gas dimethyl sulfide (DMS). DMSO can be produced through the transformation of DMS by both photooxidation and biooxidation routes or by direct production from marine phytoplankton. The formation of DMSO therefore leads to the removal of DMS from seawater, effectively controlling DMS flux into the atmosphere. In addition to its roles in protecting cells against photogenerated oxidants and cryogenic damage, DMSO can also be used as an alternative electron acceptor for energy conservation through microbial dissimilatory reduction, involving the enzyme DMSo redutase. DMSO acts as a substantial sink for DMS in deep oceanic waters. Both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship
physiological function
DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
physiological function
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dimethyl sulfoxide (DMSO) is an environmentally significant compound due to the potential role that it plays in the biogeochemical cycle of the climatically active gas dimethyl sulfide (DMS). DMSO can be produced through the transformation of DMS by both photooxidation and biooxidation routes or by direct production from marine phytoplankton. The formation of DMSO therefore leads to the removal of DMS from seawater, effectively controlling DMS flux into the atmosphere. In addition to its roles in protecting cells against photogenerated oxidants and cryogenic damage, DMSO can also be used as an alternative electron acceptor for energy conservation through microbial dissimilatory reduction, involving the enzyme DMSo redutase. DMSO acts as a substantial sink for DMS in deep oceanic waters. Both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship
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physiological function
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DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
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physiological function
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deletion mutant of catayltic subunit DmsA is attenuated in acute disease in an aerosol infection model
-
physiological function
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DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
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physiological function
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DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
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physiological function
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DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
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structure-function analysis of DMSO reductases, overview. Comparison of oxygen atom transfer (OAT) reactivity in different families of canonical pyranopterin Mo enzymes , including the DMSO reductase family, the sulfite oxidase (SO) family, the xanthine oxidase (XO) family enzymes, and the formate dehydrogenases. The active site structures and the nature of the ligands bound to the metal center appear to be fine-tuned so that the reactions catalyzed by pyranopterin Mo enzymes are close to thermoneutral. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry
additional information
structure-function analysis of DMSO reductases, overview. Comparison of oxygen atom transfer (OAT) reactivity in different families of canonical pyranopterin Mo enzymes, including the DMSO reductase family, the sulfite oxidase (SO) family, the xanthine oxidase (XO) family enzymes, and the formate dehydrogenases. The active site structures and the nature of the ligands bound to the metal center appear to be fine-tuned so that the reactions catalyzed by pyranopterin Mo enzymes are close to thermoneutral. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry
additional information
the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
additional information
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the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
additional information
two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview
additional information
two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview
additional information
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the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
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additional information
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the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
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additional information
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the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
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additional information
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the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
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