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Nutrients Dec 2021Molybdenum has been found to be associated with metabolic disorders. However, the relationship between molybdenum and metabolic syndrome (MetS) is still unclear. A large...
Molybdenum has been found to be associated with metabolic disorders. However, the relationship between molybdenum and metabolic syndrome (MetS) is still unclear. A large case-control study was conducted in a Chinese population from the baseline of Ezhou-Shenzhen cohort. A total of 5356 subjects were included with 2678 MetS and 2678 controls matched by sex and age (±2 years). Medians (IQRs) of plasma molybdenum concentrations were 1.24 μg/L for MetS cases and 1.46 μg/L for controls. After adjustment for multiple covariates, the odds ratio (OR) and 95% confidence intervals (CIs) for MetS were 1.00 (reference), 0.71 (0.59-0.84), 0.56 (0.46-0.68), and 0.47 (0.39-0.58) across quartiles of plasma molybdenum, and per SD increment of log-transformed molybdenum was associated with a 23% lower risk of MetS. In the spline analysis, the risk of MetS and its components decreased steeply with increasing molybdenum and followed by a plateau when the cutoff point was observed around 2.0 μg/L. The dose-dependent relationship of molybdenum with MetS remained consistent when considering other essential elements in the Bayesian kernel machine regression (BKMR) model. In our study, higher plasma molybdenum was significantly associated with a lower risk of MetS, as well as its components, in a dose-response manner.
Topics: Adult; Age Factors; Asian People; Biomarkers; Case-Control Studies; Coenzymes; Cohort Studies; Female; Humans; Male; Metabolic Syndrome; Middle Aged; Molybdenum; Risk
PubMed: 34960095
DOI: 10.3390/nu13124544 -
Journal of Biological Inorganic... Feb 2022Ethylbenzene dehydrogenase (EbDH), the initial enzyme of anaerobic ethylbenzene degradation from the beta-proteobacterium Aromatoleum aromaticum, is a soluble...
Ethylbenzene dehydrogenase (EbDH), the initial enzyme of anaerobic ethylbenzene degradation from the beta-proteobacterium Aromatoleum aromaticum, is a soluble periplasmic molybdenum enzyme consisting of three subunits. It contains a Mo-bis-molybdopterin guanine dinucleotide (Mo-bis-MGD) cofactor and an 4Fe-4S cluster (FS0) in the α-subunit, three 4Fe-4S clusters (FS1 to FS3) and a 3Fe-4S cluster (FS4) in the β-subunit and a heme b cofactor in the γ-subunit. Ethylbenzene is hydroxylated by a water molecule in an oxygen-independent manner at the Mo-bis-MGD cofactor, which is reduced from the Mo to the Mo state in two subsequent one-electron steps. The electrons are then transferred via the Fe-S clusters to the heme b cofactor. In this report, we determine the midpoint redox potentials of the Mo-bis-MGD cofactor and FS1-FS4 by EPR spectroscopy, and that of the heme b cofactor by electrochemically induced redox difference spectroscopy. We obtained relatively high values of > 250 mV both for the Mo-Mo redox couple and the heme b cofactor, whereas FS2 is only reduced at a very low redox potential, causing magnetic coupling with the neighboring FS1 and FS3. We compare the results with the data on related enzymes and interpret their significance for the function of EbDH.
Topics: Electron Spin Resonance Spectroscopy; Iron-Sulfur Proteins; Molybdenum; Oxidation-Reduction; Oxidoreductases
PubMed: 34843002
DOI: 10.1007/s00775-021-01917-0 -
Nutrition Research Reviews Dec 2011The rumen is the site of significant interactions between Cu, S and Mo. It also shows reactions between Cu, S and Fe. The interaction between Mo and S results in the... (Review)
Review
The rumen is the site of significant interactions between Cu, S and Mo. It also shows reactions between Cu, S and Fe. The interaction between Mo and S results in the formation of thiomolybdates, which in the absence of adequate quantities of rumen Cu are absorbed into the animal and bind to Cu in biological compounds. This is the cause of thiomolybdate toxicity, often misleadingly called Cu deficiency. The effects of thiomolybdates being absorbed into the animal are considered, especially how thiomolybdates bind to Cu-containing compounds such as enzymes, decreasing their activity without removing the active Cu component. The sources of Cu, Mo, Fe and S are examined, including the impacts of water and soil on the animal's intake. Within the present review we have been able to provide evidence that: all classes of thiomolybdates are formed in the rumen; in the absence of available Cu all thiomolybdates can be absorbed into the animal rapidly though the rumen wall or via the small intestine; thiomolybdates bind to Cu in biological compounds and are able to cause problems; effects of thiomolybdate are reversible in vivo and in vitro on cessation of thiomolybdate challenge; the tetra-thiomolybdate form is the most potent Cu binder with decreased potency with decreasing S in the compound. Fe will exacerbate a thiomolybdate problem but will not directly cause it.
Topics: Absorption; Animals; Copper; Intestinal Absorption; Iron; Molybdenum; Rumen; Ruminants; Soil; Sulfur; Water
PubMed: 22296933
DOI: 10.1017/S0954422411000059 -
Journal of Comparative Pathology Oct 2022Molybdate (MoO) and tetrathiomolybdate (MoS) supplementation of rats via drinking water had opposite effects on the establishment of Nippostrongylus brasiliensis larvae...
Effects of Molybdate and Tetrathiomolybdate Supplementation of Drinking Water on Immature Rats Infected with Nippostrongylus brasiliensis. 2. Copper Status and Tissue Molybdenum Accretion.
Molybdate (MoO) and tetrathiomolybdate (MoS) supplementation of rats via drinking water had opposite effects on the establishment of Nippostrongylus brasiliensis larvae but both induced hypercupraemia, temporarily inhibited activities of superoxide dismutase in liver and duodenum after infection and enlarged the femoral head. Effects of MoO and MoS on activities of caeruloplasmin oxidase (CpO) in plasma, erythrocyte superoxide dismutase (ESOD) and tissue copper (Cu) and molybdenum (Mo) were compared to test the hypothesis that species lacking a rumen can thiolate MoO. Three groups of 18 immature Wistar rats were given Mo (70 mg/L as MoO) or MoS (5 mg/L) via drinking water or remained untreated; all received a commercial, cubed diet and 12 from each group were infected with larvae of N. brasiliensis. Rats were killed 7-9 days later and liver, kidney, spleen, heart, muscle (quadriceps), brain and bone (femur) removed for Cu and Mo analysis. Plasma Cu was greatly increased by MoO and MoS, without changing CpO activity, but the effect was more variable with MoO and accompanied by a smaller decrease in ESOD. Tissue Cu and Mo were increased by MoS in all tissues examined except brain and bone, correlating with plasma Cu and with each other; relationships were strongest in spleen, followed by kidney. MoO also increased soft tissue Cu and Mo but increases were generally smaller than those induced by MoS and correlations between the two elements and with plasma Cu generally weaker. Since hypercupraemia and correlated increases in liver and kidney Cu and Mo are characteristic of systemic thiomolybdate (TM) exposure, we conclude that MoO was partially thiolated to give a different TM profile from that produced by MoS. The pathophysiological significance of systemic exposure to di- and tri-TM merits investigation in non-ruminants as agents of chelation therapy and in ruminants as agents of short-lived TM toxicity on Mo-rich pastures.
Topics: Animals; Ceruloplasmin; Copper; Dietary Supplements; Drinking Water; Liver; Molybdenum; Nippostrongylus; Rats; Rats, Wistar; Superoxide Dismutase
PubMed: 36209706
DOI: 10.1016/j.jcpa.2022.08.001 -
Molecules (Basel, Switzerland) Oct 2020Raman spectroscopy was used for the quantitative determination of Mo and W in Mo- and W-supported mesoporous silica (Mo/SBA-15 and W/SBA-15, respectively) and...
Raman spectroscopy was used for the quantitative determination of Mo and W in Mo- and W-supported mesoporous silica (Mo/SBA-15 and W/SBA-15, respectively) and Mo-supported beta zeolite (Mo-BEA). Three Raman quantitative models were developed and optimized for the metal contents of Mo/SBA-15, W/SBA-15, and Mo/BEA. Subsequently, the models were characterized using the root mean square error of calibration (RMSEC), root mean square error of cross-validation (RMSECV), root mean square error of prediction (RMSEP), correlation coefficient, and predicted residual error sum of squares (PRESS) diagnostic function. The calibration range of the models were in the range of approximately 2-40 wt% for the SBA-15 support and 1-21 wt% for the BEA support because the BEA support presented lower Mo absorption than the SBA-15 support. The RMSEC, RMSECV, and RMSEP values were below 1.80% for all developed models. The highest and lowest correlation coefficients corresponded to the W/SBA-15 (0.9984) and Mo/BEA (0.9777) models, respectively. The change in catalyst support affected the mentioned chemometric parameters (Mo/SBA-15 vs. Mo/BEA). Subsequently, Raman spectroscopy combined with the temperature control stage was used to study the calcination of Mo/BEA, Mo/SBA-15, and W/SBA-15 using three-dimensional diagrams, in which the changes in catalyst structure were analyzed as functions of the temperature and time. Raman spectroscopy was determined to be a suitable analytical tool for the quantitative analysis of the metal contents of the catalyst and optimization of the calcination process. Therefore, Raman spectroscopy can be used during catalyst manufacturing.
Topics: Molybdenum; Porosity; Silicon Dioxide; Spectrum Analysis, Raman; Tungsten; Zeolites
PubMed: 33114259
DOI: 10.3390/molecules25214918 -
Microbiology and Molecular Biology... Dec 2011Nitrogenase catalyzes a key step in the global nitrogen cycle, the nucleotide-dependent reduction of atmospheric dinitrogen to bioavailable ammonia. There is a... (Review)
Review
Nitrogenase catalyzes a key step in the global nitrogen cycle, the nucleotide-dependent reduction of atmospheric dinitrogen to bioavailable ammonia. There is a substantial amount of interest in elucidating the biosynthetic mechanisms of the FeMoco and the P-cluster of nitrogenase, because these clusters are not only biologically important but also chemically unprecedented. In this review, we summarize the recent advances in this research area, with an emphasis on our work that aims at providing structural and spectroscopic insights into the assembly of these complex metalloclusters.
Topics: Metalloproteins; Molybdenum; Nitrogenase; Protein Biosynthesis
PubMed: 22126998
DOI: 10.1128/MMBR.05008-11 -
Chemistry (Weinheim An Der Bergstrasse,... Feb 2022Nitrogenase is the only enzyme in nature that can fix N from the air. The active cofactor of the leading form of this enzyme contains seven irons and one molybdenum...
Nitrogenase is the only enzyme in nature that can fix N from the air. The active cofactor of the leading form of this enzyme contains seven irons and one molybdenum connected by sulfide bridges. In several recent experimental studies, it has been suggested that the cofactor is very flexible, and might lose one of its sulfides during catalysis. In this study, the possible loss of a sulfide has been investigated by model calculations. In previous studies, we have shown that there should be four activation steps before catalysis starts, and this study is based on that finding. It was found here that, after the four reductions in the activation steps, a sulfide will become very loosely bound and can be released in a quite exergonic step with a low barrier. The binding of N has no part in that release. In our previous studies, we suggested that the central carbide should be protonated three times after the four activation steps. With the new finding, there will instead be a loss of a sulfide, as the barrier for the loss is much lower than the ones for protonating the carbide. Still, it is suggested here that the carbide will be protonated anyway, but only with one proton, in the E to E step. A very complicated transition state for H formation involving a large structural change was obtained. The combined step, with a loss of H and binding of N , is calculated to be endergonic by +2.3 kcal mol ; this is in excellent agreement with experiments in which an easily reversible step has been found.
Topics: Molybdenum; Nitrogen; Nitrogenase; Oxidation-Reduction; Protons; Sulfides
PubMed: 35098591
DOI: 10.1002/chem.202103745 -
Angewandte Chemie (International Ed. in... Dec 2022Alkene metathesis catalyzed by enantiopure metal alkylidene complexes enables exceptionally versatile strategies to products with configurationally-defined...
Alkene metathesis catalyzed by enantiopure metal alkylidene complexes enables exceptionally versatile strategies to products with configurationally-defined stereocenters. Desymmetrization processes thereby provide reliable stereoselective routes to aliphatic structures, while the differentiation of aromatic stereogenic units remained an outstanding challenge. Herein, we describe the feasibility of alkene metathesis to catalytically control stereogenic axes by traceless arene formation. Stereodynamic trienes are selectively converted into corresponding binaphthalene atropisomers upon exposure to a chiral molybdenum catalyst. Remarkably, stereoselective arene-forming metathesis allows enantioselectivities of up to 98 : 2 e.r. and excellent yields. As the disconnection of each bond of an aromatic target is retrosynthetically conceivable, it is anticipated that forging arenes by means of stereoselective metathesis will enable versatile approaches for the synthesis of a broad range of molecular topologies with precisely defined configuration.
Topics: Alkenes; Stereoisomerism; Catalysis; Molybdenum; Coordination Complexes
PubMed: 36283028
DOI: 10.1002/anie.202211168 -
Dalton Transactions (Cambridge, England... Feb 2013Substitutions of trans-Na(Him)[Mo(2)O(4)(ox)(2)(H(2)O)(2)]·H(2)O (1) and trans-(Him)(2)[Mo(2)O(4)(ox)(2)(H(2)O)(2)] (2) with imidazole result in the formation of the...
Substitutions of trans-Na(Him)[Mo(2)O(4)(ox)(2)(H(2)O)(2)]·H(2)O (1) and trans-(Him)(2)[Mo(2)O(4)(ox)(2)(H(2)O)(2)] (2) with imidazole result in the formation of the mixed-ligand molybdenum complexes cis-Na(2)[Mo(2)O(4)(ox)(2)(im)(2)]·4.5H(2)O (3), cis-K(2)[Mo(2)O(4)(ox)(2)(im)(2)]·3H(2)O (4), respectively (H(2)ox = oxalic acid; im = imidazole). Further reduction of cis-K(2)[Mo(2)O(4)(ox)(2)(im)(2)]·3H(2)O (4) gives a trinuclear molybdenum(IV) complex K(Him)[Mo(3)O(4)(ox)(3)(im)(3)]·3H(2)O (5), which contains an incomplete cubane cluster [Mo(IV)(3)O(4)](4+). Two novel trinuclear mixed-valence imidazole compounds [Mo(3)O(8)(im)(4)](im)·H(2)O (6) and [Mo(3)O(8)(im)(4)]·H(2)O (7) were obtained by the reduction of (Him)(4)[Mo(8)O(26)(im)(2)] (8). Both 6 and 7 contain a novel Mo(VI)O(4)(Mo(V)(2)O(4)) center, where the [Mo(V)(2)O(4)](2+) unit is linked by [Mo(VI)O(4)](2-) anion. The Mo-Mo bond distances in 1-7 decrease with the decrease of oxidation state of molybdenum. Solid and solution NMR spectra show that imidazole molybdenum compounds 6-8 fully dissociate in solution, where solvated imidazole and imidazolium groups in 6 and 8 could be served as internal references in their solid (13)C NMR spectra. Furthermore, mixed-ligand molybdenum species 3 and 4 are stable in water. Stabilities of 3 and 4 in solution may be attributed to the strong coordination of bidentate oxalate and the formation of hydrogen bond. Dimers 2 and 4 display quasi-reversible redox process, while trimer 6 is irreversible. Bond valence calculations for 1-8 are consistent with their oxidation states of molybdenum atoms. Calculation of the oxidation state in recent structure of iron molybdenum cofactor [MoFe(7)S(9)C(R-homocit)] (FeMo-co) is 3.318.
Topics: Coordination Complexes; Crystallography, X-Ray; Dimerization; Imidazoles; Ligands; Molecular Conformation; Molybdenum; Oxidation-Reduction
PubMed: 23143282
DOI: 10.1039/c2dt31566a -
The Biochemical Journal May 2018The molybdenum cofactor (Moco) is a redox-active prosthetic group found in the active site of Moco-dependent enzymes, which are vitally important for life. Moco...
The molybdenum cofactor (Moco) is a redox-active prosthetic group found in the active site of Moco-dependent enzymes, which are vitally important for life. Moco biosynthesis involves several enzymes that catalyze the subsequent conversion of GTP into cyclic pyranopterin monophosphate (cPMP), molybdopterin (MPT), adenylated MPT (MPT-AMP), and finally Moco. While the underlying principles of cPMP, MPT, and MPT-AMP formation are well understood, the molybdenum insertase (Mo-insertase)-catalyzed final Moco maturation step is not. In the present study, we analyzed high-resolution X-ray datasets of the plant Mo-insertase Cnx1E that revealed two molybdate-binding sites within the active site, hence improving the current view on Cnx1E functionality. The presence of molybdate anions in either of these sites is tied to a distinctive backbone conformation, which we suggest to be essential for Mo-insertase molybdate selectivity and insertion efficiency.
Topics: Amino Acid Sequence; Binding Sites; Catalysis; Catalytic Domain; Coenzymes; Eukaryota; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutation; Protein Conformation; Pteridines; Sequence Homology
PubMed: 29717023
DOI: 10.1042/BCJ20170935