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Molybdenum oxidases

Biochemistry of Xanthine Oxidase and Other Molybdenum Oxidases... [Pg.364]

An additional crucial piece of information emerges from the alloxan-thine study (24). Thus, it was shown that one alloxanthine binds to the enzyme per active molybdenum site. This result clearly implies that the molybdenum site is mononuclear. If a dinuclear site were involved, then it would be unlikely to require two alloxanthine molecules for inhibition and would be expected to be at least partially inhibited with one alloxan-thine/two molybdenum. Also, a difference in binding constant would be expected for the second compared with the first bound alloxanthine, but none is found. This result, coupled with the lack of evidence for Mo(V)-Mo(V) spin-spin interactions in the EPR spectra, clearly implicates a mononuclear site, and it would seem that xanthine oxidase possesses two full catalytic units, each containing one molybdenum, one flavin, and two Fe2S2 units (20). Other molybdenum oxidases also contain paired prosthetic groups and subunits, and it is likely that they each have two catalytic units per molecule. [Pg.366]

Compared with other transition metals in biological redox systems, the oxidation states likely to be used by molybdenum are very high (74). As discussed previously, the IV, V, and VI states are a likely set of participants in molybdenum oxidases, and while the II and III states remain viable for molybdenum reductases, it nevertheless seems likely that higher oxidation states will be found in these enzymes as well. Indeed, the substitution of tungsten for molybdenum in both nitrate reductase and nitrogenase indicates this likelihood as it is much more difficult to obtain the lower oxidation states of tungsten. [Pg.369]

For the molybdenum oxidases, the reverse oxo transfer reaction can be postulated wherein an oxomolybdenum( VI) species donates oxo to substrate. For example, the oxidation of aldehydes (Reaction 18) can... [Pg.375]

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). [Pg.387]

Deficiency or Toxicity in Humans. Molybdenum deficiency in humans results in deranged metaboHsm of sulfur and purines and symptoms of mental disturbances (130). Toxic levels produce elevated uric acid in blood, gout, anemia, and growth depression. Faulty utiH2ation results in sulfite oxidase deficiency, a lethal inborn error. [Pg.387]

In animal metabolism, oxomolybdoenzymes catalyse a number of oxidation processes. These oxidases contain Mo coordinated to terminal O and S atoms, and their action appears to involve loss of an O or S atom along with reduction to Mo or Mo". It is, however, the role of molybdenum in nitrogen fixation which has received most attention. [Pg.1035]

Complexes of molybdenum and tungsten with bidentate sulfur ligands have been investigated extensively. In recent years, the work in this field has been escalated by the impetus of designing models of such bioinorganic enzymes as nitrogenase and xanthine oxidase (125). The early work reviewed by Coucouvanis (1) dealt exclusively with the isolation of oxomolybdenum(V) and -(VI) species. [Pg.224]

Romao MJ, Huber R (1998) Structure and Function of the Xanthine-Oxidase Family of Molybdenum Enzymes. 90 69-96 Rosenzweig A, see Penneman RA (1973) 13 1-52... [Pg.254]

The enzymes that utilize molybdenum can be grouped into two broad categories (1) the nitrogenases, where Mo is part of a multinu-clear metal center, or (2) the mononuclear molybdenum enzymes, such as xanthine oxidase (XO), dimethyl sulfoxide (DMSO) reductase, formate dehydrogenase (FDH), and sulfite oxidase (SO). The last... [Pg.395]

Another Mossbauer study on molybdenum hydroxylases was performed on a nonenriched sample of milk xanthine oxidase (219), and an unusually large AEq (3.2 mm/s at 175 K) was also observed for the ferrous site of one of the clusters. [Pg.402]

Stephan I, B Tshisuaka, S Fetzer, F Lingens (1996) Quinaldine 4-oxidase from Arthrobacter sp. Ru61a, a versatile procaryotic molybdenum-containing hydroxylase active towards N-containing heterocyclic compounds and aromatic aldehydes. Eur J Biochem 236 155-162. [Pg.145]

Deficiency of molybdenum cofactor can lead to sulphite oxidase deficiency (Anke and Glei 1994). [Pg.203]

V. Milk Xanthine Oxidase Studies on the Role of Molybdenum. 117... [Pg.109]

Of the mammalian enzymes, the sulphite oxidase of bovine liver has only recently been discovered to contain molybdenum (15). The better known molybdenum enzymes, xanthine oxidase from cows milk (31) and aldehyde oxidase from rabbit liver (16) are closely related to one another as they are to the xanthine dehydrogenases from chicken liver (17) and from bacteria (18). [Pg.112]

Of experimental methods for studying the metal in enzymes, light absorption in the visible region from molybdenum chromophores is likely to be weak and frequently masked by stronger absorption from other enzyme constituents. Indeed only recently has a small molybdenum contribution to the absorption spectrum of even the most studied of these enzymes, xanthine oxidase, been demonstrated 33, see Section V F). [Pg.113]

Studies bearing on the role of molybdenum in enzymes will be exemplified by a detailed summary of results on the most studied of these enzymes, which is undoubtedly milk xanthine oxidase. To put this in its context, it will be preceded by a review of the general properties of xanthine oxidase. The final section will then be a short account of work on some of the other molybdenum enzymes. [Pg.114]

The feature of xanthine oxidase which is no doubt of the greatest chemical interest, is the presence of several non-protein components. Much effort has been expended in attempting to elucidate the respective roles of iron, flavin and molybdenum in the various enzyme catalysed reactions. Numerous studies of the iron constituent have been made of late (45, 46, 47, 48, 49, 50), it having been found to be of the iron-sulphur (51 a, 51 b) type. Neither iron (19) nor molybdenum (31) can be removed reversibly from the enzyme, though the FAD can be (52, see below). [Pg.115]

In the original rapid-freezing work on xanthine oxidase (53) it was found that in experiments employing about 1 mole of xanthine per mole of enzyme and an excess of oxygen, the time sequence of appearance of the various EPR signals was molybdenum (V), followed by flavin semi-quinone radical (FADH), followed by iron. This suggested that the electron transfer sequence might be ... [Pg.115]

Scheme 1. Possible oxidation-reduction reactions between reducing and oxidizing substrate molecules (R and O respectively) and the molybdenum (M), flavin (F) and iron (I) of xanthine oxidase. The enzyme molecule is represented by the circle and arrows indicate transfer of reducing equivalents... Scheme 1. Possible oxidation-reduction reactions between reducing and oxidizing substrate molecules (R and O respectively) and the molybdenum (M), flavin (F) and iron (I) of xanthine oxidase. The enzyme molecule is represented by the circle and arrows indicate transfer of reducing equivalents...
Since studies bearing on the role of molybdenum in milk xanthine oxidase have depended heavily on the EPR method, it is convenient to precede detailed discussion by a general description of the various molyb-denum(V) EPR signals which have been obtained from the enzyme. [Pg.119]


See other pages where Molybdenum oxidases is mentioned: [Pg.1355]    [Pg.365]    [Pg.366]    [Pg.367]    [Pg.3194]    [Pg.1355]    [Pg.365]    [Pg.366]    [Pg.367]    [Pg.3194]    [Pg.476]    [Pg.24]    [Pg.79]    [Pg.98]    [Pg.120]    [Pg.227]    [Pg.248]    [Pg.396]    [Pg.399]    [Pg.400]    [Pg.400]    [Pg.465]    [Pg.466]    [Pg.87]    [Pg.129]    [Pg.389]    [Pg.112]    [Pg.116]    [Pg.117]    [Pg.118]    [Pg.119]    [Pg.121]   
See also in sourсe #XX -- [ Pg.365 ]




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Aldehyde oxidase molybdenum

Carbon monoxide oxidase molybdenum

Desulfoxanthine oxidase molybdenum

Molybdenum enzymes xanthine oxidase

Molybdenum hydroxylase xanthine oxidase

Oxidation states, molybdenum center sulfite oxidase

Sulfite oxidase molybdenum cofactor

Sulfite oxidase molybdenum enzymes

Sulfite oxidase molybdenum-tungsten enzymes

Xanthine oxidase families molybdenum hydroxylase

Xanthine oxidase families molybdenum hydroxylases

Xanthine oxidase molybdenum

Xanthine oxidase molybdenum center

Xanthine oxidase molybdenum cofactor

Xanthine oxidase molybdenum complex center

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