Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). a menaquinone + dimethyl sulfide + H2O = a menaquinol + dimethyl sulfoxide.
MSNFNQISRRDFVKASSAGAALAVSNLTLPFNVMAKETQRLNENNQERIVWSACTVNCGS
RCPLRMHVKDNRITYVETDNTGTETYNLDHQVRACLRGRSMRRRVYNPDRLKYPMKRIGK
RGEGKFKRISWDEALTEIADALKRNIKKYGNESIYLNYGTGTLGGTMAKSWPPASTMIAR
FMNCIGGYLNHYGDYSTAQIAVGLDYTYGGGWALGNGMADIENTKLIVLFGNNPAETRMS
GGGLTYCIEQAKARSNAKMIIIDPRYNDTGAGREDEWIPIRPGTDAALVAALAYVMIQEN
LVDQPFLDKYCVGYDEKTLPTDAPKNGHYKAYILGYGNDGIAKTPEWAAKITGIPAERII
KLAREIGSTKPAFISQGWGPQRRSNGELISRAIAMLPILTGNVGIHGGNTGARESAYSIP
FVRMPTLKNPVKASIPMFLWTDAIIRGTEMTALTDGIRGVDKLSSPIKVIWNYASNCLIN
QHAQINRTHDILQDDTQCEMIITIDNHMTSTAKYSDILLPDCTTSEQMDFALDAFVSNMA
YVIFADQVIKPSFECRPIYDMLSDLAEKMGVKEKFTEGRTQEEWLRHIYEQSREKLPELP
TFEEFRQQGIFKKVDPNGFKVAYKDFRDNPEAHPLKTPSGKIEIYSSRLAEIAKTWKLAE
DDVIHPLPIHAQSFEHYGDPLMEKYPLQLSGFHYKARTHSTYGNVDVLKAANPQEVWMNP
IDAEPRNIKNGDMIRIFNDRGEVHINVKITPRIIPGVVALSEGAWYAPDKDRIDHSGCIN
VLTTQRPSPLAKGNPQHSNLVQVERL819
| 10224050 | Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase.Rothery RA, Trieber CA, Weiner JH | We have used site-directed mutagenesis to study the interactions between the molybdo-bis(molybdopterin guanine dinucleotide) cofactor (Mo-bisMGD) and the other prosthetic groups of Escherichia coli Me2SO reductase (DmsABC). In redox-poised preparations, there is a significant spin-spin interaction between the reduced Em,7 = -120 mV [4Fe-4S] cluster of DmsB and the Mo(V) of the Mo-bisMGD of DmsA. This interaction is significantly modified in a DmsA-C38S mutant that contains a [3Fe-4S] cluster in DmsA, suggesting that the [3Fe-4S] cluster is in close juxtaposition to the vector connecting the Mo(V) and the Em,7 = -120 mV cluster of DmsB. In a DmsA-R77S mutant, the interaction is eliminated, indicating the importance of this residue in defining the interaction pathway. In ferricyanide-oxidized glycerol-inhibited DmsAC38SBC, there is no detectable interaction between the oxidized [3Fe-4S] cluster and the Mo-bisMGD, except for a minor broadening of the Mo(V) spectrum. In a double mutant, DmsAS176ABC102SC, which contains an engineered [3Fe-4S] cluster in DmsB, no significant paramagnetic interaction is detected between the oxidized [3Fe-4S] cluster and the Mo(V). These results have important implications for (i) understanding the magnetic interactions between the Mo(V) and other paramagnetic centers and (ii) delineating the electron transfer pathway from the [4Fe-4S] clusters of DmsB to the Mo-bisMGD of DmsA. | 1999 | |
| 0 | 15716436 | Genomic analysis of anaerobic respiration in the archaeon Halobacterium sp. strain NRC-1: dimethyl sulfoxide and trimethylamine N-oxide as terminal electron acceptors.Jochen A Müller 1, Shiladitya DasSarma | We have investigated anaerobic respiration of the archaeal model organism Halobacterium sp. strain NRC-1 by using phenotypic and genetic analysis, bioinformatics, and transcriptome analysis. NRC-1 was found to grow on either dimethyl sulfoxide (DMSO) or trimethylamine N-oxide (TMAO) as the sole terminal electron acceptor, with a doubling time of 1 day. An operon, dmsREABCD, encoding a putative regulatory protein, DmsR, a molybdopterin oxidoreductase of the DMSO reductase family (DmsEABC), and a molecular chaperone (DmsD) was identified by bioinformatics and confirmed as a transcriptional unit by reverse transcriptase PCR analysis. dmsR, dmsA, and dmsD in-frame deletion mutants were individually constructed. Phenotypic analysis demonstrated that dmsR, dmsA, and dmsD are required for anaerobic respiration on DMSO and TMAO. The requirement for dmsR, whose predicted product contains a DNA-binding domain similar to that of the Bat family of activators (COG3413), indicated that it functions as an activator. A cysteine-rich domain was found in the dmsR gene, which may be involved in oxygen sensing. Microarray analysis using a whole-genome 60-mer oligonucleotide array showed that the dms operon is induced during anaerobic respiration. Comparison of dmsR+ and DeltadmsR strains by use of microarrays showed that the induction of the dmsEABCD operon is dependent on a functional dmsR gene, consistent with its action as a transcriptional activator. Our results clearly establish the genes required for anaerobic respiration using DMSO and TMAO in an archaeon for the first time. | 2005 |
Rothery R A , Trieber C A , Weiner J H . Interactions between the Molybdenum Cofactor and Iron-Sulfur Clusters of Escherichia coli Dimethylsulfoxide Reductase[J]. Journal of Biological Chemistry, 1999, 274(19):13002-13009.