Iron molybdenum containing

Nitrogen fixation is the conversion of N2 gas into ammonia, a process carried out by some soil bacteria, cyanobacteria and the symbiotic bacteria Rhizobium that invade the root nodules of leguminous plants. This process is carried out by the nitrogenase complex, which consists of a reductase and an iron-molybdenum-containing nitrogenase. At least 16 ATP molecules are hydrolyzed to form two molecules of ammonia. Leghemoglobin is used to protect the nitrogenase in the Rhizobium from inactivation by 02. 

It is doubtful whether the irons have any useful resistance to hydrochloric acid solutions at any concentration or temperature. It has, however, been claimed that the molybdenum-containing alloy is attacked by 1% acid at... 

The set of Mo(V) EPR signals detected in D. gigas and D. desulfuricans AORs shows close homology with the molybdenum-containing hydroxylase group. Mossbauer and X/Q-band EPR spectroscopic studies 208, 216) complemented the UV/visible and CD studies and the assignment of the [2Fe-2S] arrangement of the iron-sulfur cores. 

Next, let the example of vanadium, which, in the as-reduced condition, may contain a variety of impurities (including aluminum, calcium, chromium, copper, iron, molybdenum, nickel, lead, titanium, and zinc) be considered. Vanadium melts at 1910 °C, and at this temperature it is considerably less volatile than many of the impurity metals present in it. The vapor pressure of pure vanadium at this temperature is 0.02 torr, whereas those of the impurity elements in their pure states are the following aluminum 22 torr calcium 1 atm, chromium 6 torr copper 23 torr iron 2 torr molybdenum 6 1CT6 torr nickel 1 torr lead 1 torr titanium 0.1 torr and zinc 1 atm. However, since most of these impurities form a dilute solution in vanadium, their actual partial pressures over vanadium are considerably lower than the values indicated. Taking this into account, the vaporization rate, mA, of an element A (the evaporating species) can be approximated by the following free evaporation equation (Langmuir equation) ... 

Xanthine oxidoreductase (XOR) is a molybdenum-containing complex homodimeric 300-kDa cytosolic enzyme. Each subunit contains a molybdopterin cofactor, two nonidentical iron-sulfur centers, and FAD (89). The enzyme has an important physiologic role in the oxidative metabolism of purines, e.g., it catalyzes the sequence of reactions that convert hypoxanthine to xanthine then to uric acid (Fig. 4.36). 

Originally the FeMoco was reported to contain iron, molybdenum and sulfide in a 8 1 6 atomic ratio (2). Subsequent analytical determinations gave Fe/Mo ratios of 7 1 (3) and 8.2 0.4 1 (4). The most recent analytical data on functional FeMoco, isolated by a mild procedure, indicates (5) a Fe/Mo ratio of 5 0.5 1. A similar fluctuation in analytical results is also apparent in several determinations of sulfur content, and ratios of S/Mo as low as 4 1 (3) and as high as 9 or 8.T (4) have been reported. 

Fe2S2] clusters are part of the molybdenum containing hydroxylases. Typically, apart from molybdenum and two EPR-distinct iron-sulfur centres there can be FAD as additional cofactor. In Chlostridium purinolyticum a selenium-dependent purine hydroxylase has been characterized as molybdenum hydroxylase. The EPR of the respective desulfo molybdenum (V) signal indicated that the Mo-ligands should differ from those of the well known mammalian corollary xanthine oxidase.197 For the bacterial molybdenum hydroxylase quinoline oxidoreductase from Pseudomonas putida an expression system was developed in order to be able to construct protein mutants for detailed analysis. EPR was used to control the correct insertion of the cofactors, specifically of the two [Fe2S2] clusters.198... 

J. C. Swann Molybdenum-Containing Enzymes. - J. B. Neilands Evolution of Biological Iron Binding Centers. 

Coughlan, M. P. 1980. Aldehyde oxidase, xanthine oxidase and xanthine dehydrogenase. Hydroxylases containing molybdenum, iron-sulphur and flavin. In Molybdenum and Molybdenum-Containing Enzymes. M.P. Coughlan (Editor). Pergamon Press, Oxford, pp. 119-185. 

Nitrogenase, which catalyzes the reduction of N2 to two molecules of NH3, has a different molybdenum -iron cofactor (FeMo-co). It can be obtained by acid denaturation of the very oxygen-labile iron-molybdenum protein of nitrogenase followed by extraction with d i methyl formamide.655,656 The coenzyme is a complex Fe-S-Mo cluster also containing homocitrate with a composition MoFe7S9-homocitrate (see Fig. 24-3). Nitrogenase and this coenzyme are considered further in Chapter 24. 

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