Molybdenum redox reactions

Molybdenum. Molybdenum is a component of the metaHoen2ymes xanthine oxidase, aldehyde oxidase, and sulfite oxidase in mammals (130). Two other molybdenum metaHoen2ymes present in nitrifying bacteria have been characteri2ed nitrogenase and nitrate reductase (131). The molybdenum in the oxidases, is involved in redox reactions. The heme iron in sulfite oxidase also is involved in electron transfer (132). 

Phthalocyanines are excellent lubricants at temperatures of 149—343°C (191). Combinations with other lubricants, like grease, molybdenum, or tungsten sulfides, have found appHcations in the automotive industry or professional drilling equipment (192—195). Further uses include indicators for iron(Il), molybdenum(V), and uranium(IV) (196) or redox reactions (197), medical appHcations like hemoglobin replacements (198) or sterilisation indicators (199), or uses like in gas filters for the removal of nitrogen oxides from cigarette smoke (200). 

In summary, we may add that bacterial utilization of quinoline and its derivatives as a rule depends on the availability of traces of molybdate in the culture medium [363], In contrast, growth of the bacterial strains on the first intermediate of each catabolic pathway, namely, the lH-2-oxo or 1 II-4-oxo derivatives of the quinoline compound was not affected by the availability of molybdate. This observation indicated a possible role of the trace element molybdenum in the initial hydroxylation at C2. In enzymes, Mo occurs as part of the redox-active co-factor, and all the Mo-enzymes involved in N-heteroatomic compound metabolism, contain a pterin Mo co-factor. The catalyzed reaction involves the transfer of an oxygen atom to or from a substrate molecule in a two-electron redox reaction. The oxygen is supplied by the aqueous solvent. Certainly, the Mo-enzymes play an important role in the initial steps of N-containing heterocycles degradation. 

The prosthetic group associated with the molybdenum atom of the molybdenum cofactor found in most molybdenum-containing enzymes except nitrogenase (See Molybdenum Cofactor). Many of these enzymes catalyze two-electron redox reactions involving the net exchange of an oxygen atom between the substrate and water. In bacterial enzymes a nucleotide is linked to the phosphoryl group. 

For a number of years, phenolic substances were dosed by colorimetric techniques, based on redox reactions usually known as Folin Ciocalteau methods, even if a number of adjustments were developed to fit different matrix characteristics. The Folin Cioalteau reagent is a mixture of phosphomolybdic and phosphotingstic acids, with molybdenum in the 6+ oxidation state and, when the reaction takes place, it is reduced to form a complex called molybdenum blue and tungsten blue. In this complex, the mean oxidation state is between 5 and 6 and the formed complex is blue so it can be read spectrophotometrically at 750 nm. 

DNA cleavage by, 43 158-159 reactions, copper proteins, 39 25 Oxo-trichloroselenates(IV), 35 270-271 Oxo-type molybdenum enzyme, see Molybdenum enzymes, pterin-containing Oxovandium (IV), solvent exchange and ligand substitution, 42 47-49 Oxyanions, Groups VIB and VIIB, redox reactions, kinetics and mechanism, 40 269-274... 

Figure 2 Precursors of macrocyclic ligands which allow redox reactions for monomeric molybdenum centres...

Using your knowledge of periodic relationships, predict wluch element might come closest to reproducing the behavior of molybdenum in niirogenuse. Recall that nitrogen fixation involves both complication and redox reactions.1 1 ... 

A number of excellent reviews have been written that address various aspects of metal-metal bonding. In particular, Cotton has contributed several eminent early reviews commensurate with his pioneering efforts in this area (54, 59, 60). More recently he reviewed quadruple bonds (56), molybdenum-molybdenum bonds (57), and multiple bond studies in his laboratory (55) in separate articles. Earlier reports discuss multiple metal-metal bonds in the context of general metal—metal bonding schemes and clusters at a time when the area was more limited in scope and therefore amenable to an encompassing survey (13, 128, 129, 164, 188, 189, 252). The redox behavior of metal-metal bonds has been reviewed by Meyer (193), and Walton has recently described ligand-induced redox reactions of strong multiple metal—metal bonds (253). 

Redox potentials of the molybdenum centers in several of the enzymes have been obtained by potentiometric titration (Table 3a). Although the substrate reaction chemistry requires the metal center to participate in net two-electron redox reactions, the simple electron-transfer reactions of the active sites occur in one-electron steps involving the MoVI/Mov and Mov/MoIV couples. Several of the molybdenum enzymes studied have MoVI/Mov and Mov/MoIV couples that differ by less than 40 mV. However, in sulfite oxidase the Movl/Mov (38 mV) and Mov/Molv (-239 mV) couples are separated by roughly 275 mV [88], In formate dehydrogenase (D. desulfuricans) the MoVI/Mov (-160 mV) and Mov/MoIV (-330 mV) couples are separated by 170 mV [89], Both the MoVI/Mov and... 

Iron-sulfur proteins contain non-heme iron and inorganic (acid-labile) sulfur in their active centers as 4Fe-4S or 2Fe-2S or, in the case of rubredoxin, as one iron alone. The iron is always bonded to cysteine sulfur. They catalyze redox reactions between +350 and —600 mV (hydrogen electrode = —420 mV). They are usually of low molecular weight (6000-15,000 Daltons) but can form complex enzymes with molybdenum and flavin. They occur as soluble or membrane-bound proteins and catalyze key reactions in photosynthesis, oxidative phosphorylation, nitrogen fixation, H2 metabolism, steroid hydroxylation, carbon and sulfur metabolism, etc. They occur in all organisms so far investigated and may... 

Molybdenum is essential to the formation and activity of assimila-tory nitrate reductases. Cells must assimilate molybdate from the environment, metabolize molybdenum in some manner to form active molybdenum cofactor, and then incorporate it into a large molecular weight protein so that it can perform a reversible redox reaction with nitrate. Investigations on the aqueous Mo (III) model systems for nitrate reduction and the coordination of molybdate by naturally produced phenolates will hopefully lead to an understanding of the complex process of molybdenum acquisitions by and molybdenum function in nitrate reductases. 

D. L. Pearsall, E. M. Moore, S. M. Blaney, and S. J. Nieter Burgmayer, Redox Reactions of the Pyranopterin System of the Molybdenum cofactor, submitted to J. Biol. Inorg. Chem. 

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