Metalloenzymes molybdenum

Metalloenzymes, 33 40, see also Enzymes crystal structure, 44 230-258 DNA repair, 45 251 inhibitors, 36 40-42 molybdenum, 45 2, 53, 60-63 nuleic acid hydrolysis, 45 251-252 superoxide dismustases and, 45 130 zinc-containing, hard and soft acid-base behavior, 42 103-109 Metalloids... 

A large number of studies devoted to metal-sulfur centers are motivated by the occurrence of such arrangements at the active site of various metalloenzymes [1-13]. Mononuclear complexes with Mo=0 func-tion(s) and possessing sulfur ligands in their coordination sphere have been extensively investigated since they can be seen as models of the active site of enzymes such as nitrate- and DM SO reductases or sulfite- and xanthine oxidases [1-4]. On the other hand, a large variety of mono-, di-, and polynuclear Mo—S centers have been synthesized in order to produce functional models of the Mo-nitrogenase since the exact nature (mono-, di- or polynuclear) of the metal center, where N2 interacts within the iron-molybdenum cofactor (FeMo—co) of the enzyme is still unknown [4-8]. 

Molybdenum 10 mg 150- 500 pig In metalloenzymes xanthine, aldehyde, sulfite oxidases Faulty metabolism of xanthine, sulfur Gout-like syndrome in parts of Soviet Union... 

Molybdenum is required in the diet. It is required by three enzymes in mammals sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. Molybdenum occurs in these enz)anes as part of the molybdenum cofactor (Figure 10.52). This cofactor is biosynthesized in the body with GTP as the starting material. AH known Mo metalloenzymes, with the exception of nitrogenase (a plant enz5une), use Mo in the form of the molybdemun cofactor. 

Tn recent years there has been an increased interest in assessing the human health effects from environmental exposure to trace metals. Studies of occupational exposures and dietary intakes of trace metals have required the refinement and development of analytical techniques for the analyses of low elemental concentrations in complex matrices. Molybdenum is one of the trace metals that has been the subject of intensive study because it is an essential trace element in both plant and animal nutrition. It is an integral constituent of several metalloenzymes including xanthine oxidase, which is the last enzyme in the catabolic pathway of purines. Extensive ingestion of molybdenum has been shown to cause molybdenosis in cattle. Many of the features of this condition can be ascribed to induced copper deficiency. Whether biochemical changes or adverse health effects in humans can be attributed to excessive exposure to molybdenum is not known. 

VII. References to Metalloenzymes Containing Copper, Iron and Molybdenum. 332... 

A wide range of metal ions is present in metalloenzymes as cofactors. Copper zinc snperoxide dismntase is a metalloenzyme that nses copper and zinc to help catalyze the conversion of snperoxide anion to molecnlar oxygen and hydrogen peroxide. Thermolysin is a protease that nses a tightly bonnd zinc ion to activate a water atom, which then attacks a peptide bond. Aconitase is one of the enzymes of the citric acid cycle it contains several iron atoms bonnd in the form of iron-sulfur clusters, which participate directly in the isomerization of citrate to isocitrate. Other metal ions fonnd as cofactors in metalloenzymes include molybdenum (in nitrate rednctase), seleninm (in glutathione peroxidase), nickel (in urease), and vanadinm (in fungal chloroperoxidase). see also Catalysis and Catalysts Coenzymes Denaturation Enzymes Krebs Cycle. 

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