User:Adam Mirando/Sandbox 1: Difference between revisions

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'''Xanthine [http://en.wikipedia.org/wiki/Oxidoreductase oxidoreductase]''' (XOR) is an extensively studied metalloflavoprotein from the molybdenum hydroxylase family that is found in a variety of different organisms, ranging from bacteria to eukaryotes <ref>PMID:11848841</ref>. XORs are dimeric enzymes typically around 280 kDa in size with two interconvertible forms: xanthine dehydrogenase (XDH) [1.17.1.4] and xanthine oxidase (XO) [1.17.3.2]. Conversion between the two forms is mediated through the reversible oxidation of several cysteine residues or irreversible [http://en.wikipedia.org/wiki/Trypsin trypsin] truncation <ref name="structure" />. XOR is involved in purine catabolism, catalyzing the [http://en.wikipedia.org/wiki/Redox oxidation] of [http://en.wikipedia.org/wiki/Hypoxanthine hypoxanthine] and [http://en.wikipedia.org/wiki/Xanthine xanthine] to [http://en.wikipedia.org/wiki/Urate urate] through the extraction of two electrons <ref name="gluarg" />. The transport of these electrons is facilitated by the [http://en.wikipedia.org/wiki/Molybdenum molybdenum] of the <scene name='User:Adam_Mirando/Sandbox_1/Mo_pterin_domain/3'>molybdopterin cofactor</scene>, two

<scene name='User:Adam_Mirando/Sandbox_1/Fes_clusters/2'>iron sulfur centers</scene>, and a bound

<scene name='User:Adam_Mirando/Sandbox_1/Fad_domain/4'>FAD</scene> coenzyme. In XDH the electrons are then passed preferentially from the reduced [http://en.wikipedia.org/wiki/FAD flavin] to a final [http://en.wikipedia.org/wiki/Nicotinamide_adenine_dinucleotide NAD+] acceptor, creating NADH <ref name="thermo" />. Apart from NADH, XDH may also use O2 as a final electron acceptor. In contrast, conversion to the XO form precludes NAD+ from binding, permitting only the use of O2. The reduction of O2 produces substantial amounts of H2O2 and superoxide as byproducts <ref name="gluarg" /><ref name="conver">PMID:15878860</ref>. The ~~prodution~~ of these ~~oxidative species has~~ been implicated in the innate immune response <ref>PMID:12967676</ref> and cardiovascular disease, such as [http://en.wikipedia.org/wiki/Atherosclerosis atherosclerosis] <ref>PMID:12958034</ref>, [http://en.wikipedia.org/wiki/Reperfusion_injury ischemia-reperfusion injury], and chronic heart failure <ref>PMID:14694147</ref> <ref>PMID:12105162</ref>.

<scene name='User:Adam_Mirando/Sandbox_1/Fad_domain/4'>FAD</scene> coenzyme. In XDH the electrons are then passed preferentially from the reduced [http://en.wikipedia.org/wiki/FAD flavin] to a final [http://en.wikipedia.org/wiki/Nicotinamide_adenine_dinucleotide NAD+] acceptor, creating NADH <ref name="thermo" />. Apart from NADH, XDH may also use O2 as a final electron acceptor. In contrast, conversion to the XO form precludes NAD+ from binding, permitting only the use of O2. The reduction of O2 produces substantial amounts of H2O2 and superoxide as byproducts <ref name="gluarg" /><ref name="conver">PMID:15878860</ref>. The products of these enzymes have been implicated in the innate immune response as a balancer of redox potential and antioxidant (urate) provider<ref>PMID:12967676</ref> and cardiovascular disease, such as [http://en.wikipedia.org/wiki/Atherosclerosis atherosclerosis] <ref>PMID:12958034</ref>, [http://en.wikipedia.org/wiki/Reperfusion_injury ischemia-reperfusion injury], and chronic heart failure <ref>PMID:14694147</ref> <ref>PMID:12105162</ref>.

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 '''Xanthine [http://en.wikipedia.org/wiki/Oxidoreductase oxidoreductase]''' (XOR) is an extensively studied metalloflavoprotein from the molybdenum hydroxylase family that is found in a variety of different organisms, ranging from bacteria to eukaryotes <ref>PMID:11848841</ref>. XORs are dimeric enzymes typically around 280 kDa in size with two interconvertible forms: xanthine dehydrogenase (XDH) [1.17.1.4] and xanthine oxidase (XO) [1.17.3.2]. Conversion between the two forms is mediated through the reversible oxidation of several cysteine residues or irreversible [http://en.wikipedia.org/wiki/Trypsin trypsin] truncation <ref name="structure" />. XOR is involved in purine catabolism, catalyzing the [http://en.wikipedia.org/wiki/Redox oxidation] of [http://en.wikipedia.org/wiki/Hypoxanthine hypoxanthine] and [http://en.wikipedia.org/wiki/Xanthine xanthine] to [http://en.wikipedia.org/wiki/Urate urate] through the extraction of two electrons <ref name="gluarg" />. The transport of these electrons is facilitated by the [http://en.wikipedia.org/wiki/Molybdenum molybdenum] of the <scene name='User:Adam_Mirando/Sandbox_1/Mo_pterin_domain/3'>molybdopterin cofactor</scene>, two
 <scene name='User:Adam_Mirando/Sandbox_1/Fes_clusters/2'>iron sulfur centers</scene>, and a bound
-<scene name='User:Adam_Mirando/Sandbox_1/Fad_domain/4'>FAD</scene> coenzyme. In XDH the electrons are then passed preferentially from the reduced [http://en.wikipedia.org/wiki/FAD flavin] to a final [http://en.wikipedia.org/wiki/Nicotinamide_adenine_dinucleotide NAD<sup>+</sup>] acceptor, creating NADH <ref name="thermo" />. Apart from NADH, XDH may also use O<sub>2</sub> as a final electron acceptor. In contrast, conversion to the XO form precludes NAD<sup>+</sup> from binding, permitting only the use of O<sub>2</sub>. The reduction of O<sub>2</sub> produces substantial amounts of H<sub>2</sub>O<sub>2</sub> and superoxide as byproducts <ref name="gluarg" /><ref name="conver">PMID:15878860</ref>.  The prodution of these oxidative species has been implicated in the innate immune response <ref>PMID:12967676</ref> and cardiovascular disease, such as [http://en.wikipedia.org/wiki/Atherosclerosis atherosclerosis] <ref>PMID:12958034</ref>, [http://en.wikipedia.org/wiki/Reperfusion_injury ischemia-reperfusion injury], and chronic heart failure <ref>PMID:14694147</ref> <ref>PMID:12105162</ref>.
+<scene name='User:Adam_Mirando/Sandbox_1/Fad_domain/4'>FAD</scene> coenzyme. In XDH the electrons are then passed preferentially from the reduced [http://en.wikipedia.org/wiki/FAD flavin] to a final [http://en.wikipedia.org/wiki/Nicotinamide_adenine_dinucleotide NAD<sup>+</sup>] acceptor, creating NADH <ref name="thermo" />. Apart from NADH, XDH may also use O<sub>2</sub> as a final electron acceptor. In contrast, conversion to the XO form precludes NAD<sup>+</sup> from binding, permitting only the use of O<sub>2</sub>. The reduction of O<sub>2</sub> produces substantial amounts of H<sub>2</sub>O<sub>2</sub> and superoxide as byproducts <ref name="gluarg" /><ref name="conver">PMID:15878860</ref>.  The products of these enzymes have been implicated in the innate immune response as a balancer of redox potential and antioxidant (urate) provider<ref>PMID:12967676</ref> and cardiovascular disease, such as [http://en.wikipedia.org/wiki/Atherosclerosis atherosclerosis] <ref>PMID:12958034</ref>, [http://en.wikipedia.org/wiki/Reperfusion_injury ischemia-reperfusion injury], and chronic heart failure <ref>PMID:14694147</ref> <ref>PMID:12105162</ref>.