<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>1405-888X</journal-id>
<journal-title><![CDATA[TIP. Revista especializada en ciencias químico-biológicas]]></journal-title>
<abbrev-journal-title><![CDATA[TIP]]></abbrev-journal-title>
<issn>1405-888X</issn>
<publisher>
<publisher-name><![CDATA[Universidad Nacional Autónoma de México, Facultad de Estudios Superiores Zaragoza]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S1405-888X2005000100028</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Las quinoproteínas alcohol deshidrogenasas en los sistemas bacterianos: distribución, clasificación, estructura y función]]></article-title>
<article-title xml:lang="en"><![CDATA[The alcohol quinoproteins dehydrogenases in the bacterial systems: distribution, classification, structure and function]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Gómez-Manzo]]></surname>
<given-names><![CDATA[Saúl]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Arreguín-Espinosa]]></surname>
<given-names><![CDATA[Roberto]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Contreras-Zentella]]></surname>
<given-names><![CDATA[Martha]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Escamilla-Marván]]></surname>
<given-names><![CDATA[Edgardo]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,UNAM Instituto de Fisiología Celular Depto. de Bioquímica]]></institution>
<addr-line><![CDATA[México, D.F. ]]></addr-line>
<country>Mexico</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,UNAM Instituto de Química ]]></institution>
<addr-line><![CDATA[México, D.F. ]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2005</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2005</year>
</pub-date>
<volume>8</volume>
<numero>1</numero>
<fpage>28</fpage>
<lpage>37</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S1405-888X2005000100028&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S1405-888X2005000100028&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S1405-888X2005000100028&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen Existe una gran diversidad de alcohol deshidrogenasas (ADHs) microbianas; las cuales son divididas en tres grandes grupos: (a) Las que son dependientes de las coenzimas NAD o NADP, (b) Las que son independientes de estas coenzimas; sin embargo, utilizan pirroloquinolina quinona (PQQ) y hemo tipo C como grupo prostético y (c) Las oxidasas dependientes de FAD que catalizan la reacción irreversible de alcoholes. Las ADHs que utilizan el PQQ, se encuentran a su vez divididas en tres tipos. Las ADHs tipo I que contienen sólo PQQ como grupo prostético y se les conoce como quinoproteínas; mientras que las ADHs tipo II y tipo III además del PQQ contienen hemo tipo C y se les conoce como quinohemoproteínas. Las ADHs tipo II son enzimas solubles que se encuentran en el espacio periplásmico y están presentes en proteobacterias como Pseudomonas putida, Ralstonia eutropha y Comamonas testosteroni. Las ADHs tipo Ill son enzimas que se encuentran ancladas a la membrana y trabajan orientadas hacia el espacio periplásmico. se les ha identificado y caracterizado únicamente en bacterias ácido acéticas. Las ADH tipo III, por lo general contienen tres subunidades. El transporte intramolecular de electrones en las ADHs tipo II y IIII se propone que es del PQQ al hemo C de la primera subunidad y de ahí, de hemo en hemo en la segunda subunidad hasta llegar a la quinona endógena. Los tres tipos de PQQ-ADHs son discutidas en esta revisión.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract Microbial alcohol oxidoreductases constitute a very diverse group. They can be divided into three major categories. (a) NAD(P)-dependent dehydrogenases. (b) NAD(P)-independent enzymes that use pirroloquinoline quinone (PQQ), heme C as cofactor. (c) FAD-dependent oxidases that catalyze an essentially irreversible oxidation of alcohols. The ADHs that have PQQ as the prosthetic group are divided into 3 groups; types I, II and III. Type I ADH is a simple quinoprotein having PQQ as the prosthetic group; while type II and type III ADHs are quinohemoprotein having heme C as well as PQQ. Type II are soluble periplasmic enzymes and are widely distributed in Proteobacterias such as Pseudomonas putida, Ralstonia eutropha and Comamonas testosteroni. Type III ADHs are membrane-bound enzymes and oriented towards the periplasmic surface. They have been identified and characterized solely in acetic acid bacteria. Type III ADH consists of three subunits. The intramolecular electron transfer in the type II and III ADHs is the PQQ to heme C of the first subunit and there, from heme to heme in the second subunit until arriving at ubiquinone. The three types of PQQ-ADHs are discussed in this paper.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[Alcohol deshidrogenasas (ADHs)]]></kwd>
<kwd lng="es"><![CDATA[pirrolo-quinolina-quinona (PQQ)]]></kwd>
<kwd lng="es"><![CDATA[quinohemoproteína alcohol deshidrogenasa (qhADH)]]></kwd>
<kwd lng="es"><![CDATA[quinohemoproteína etanol deshidrogenasa (qhEDH)]]></kwd>
<kwd lng="es"><![CDATA[quinoproteína etanol deshidrogenasa (QEDH)]]></kwd>
<kwd lng="es"><![CDATA[quinoproteína metanol deshidrogenasa (QMDH)]]></kwd>
<kwd lng="en"><![CDATA[Alcohol dehydrogenases (ADHs)]]></kwd>
<kwd lng="en"><![CDATA[pyrroloquinoline-quinone (PQQ)]]></kwd>
<kwd lng="en"><![CDATA[quinohemeprotein alcohol dehydrogenase (qhADH)]]></kwd>
<kwd lng="en"><![CDATA[quinohemeprotein ethanol deshydrogenase (qhEDH)]]></kwd>
<kwd lng="en"><![CDATA[quinoprotein ethanol dehydrogenase (QEDH)]]></kwd>
<kwd lng="en"><![CDATA[quinoprotein methanol dehydrogenase (QMDH)]]></kwd>
</kwd-group>
</article-meta>
</front><back>
<ref-list>
<ref id="B1">
<label>1</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Jornvall]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Person]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
<name>
<surname><![CDATA[Jeffery]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Characteristics of alcohol/polyol dehydrogenases]]></article-title>
<source><![CDATA[Eur. J. Biochem]]></source>
<year>1987</year>
<volume>167</volume>
<page-range>195-201</page-range></nlm-citation>
</ref>
<ref id="B2">
<label>2</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Veenhuis]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Douma]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Harder]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
<name>
<surname><![CDATA[Osumi]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Degradation and turnover in the yeast Hansenula polymorpha induced by selective inactivation of peroxisomal enzymes]]></article-title>
<source><![CDATA[Arch. Microbiol]]></source>
<year>1983</year>
<volume>134</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>193-203</page-range></nlm-citation>
</ref>
<ref id="B3">
<label>3</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Anthony]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Zatman]]></surname>
<given-names><![CDATA[L.J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The microbial oxidation of methanol: The prostetic group of alcohol dehydrogenase of Pseudomonas]]></article-title>
<source><![CDATA[Biochem. J]]></source>
<year>1967</year>
<volume>304</volume>
<page-range>665-74</page-range></nlm-citation>
</ref>
<ref id="B4">
<label>4</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Duine]]></surname>
<given-names><![CDATA[J.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Jongejan]]></surname>
<given-names><![CDATA[J.A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Pyrroloquinoline quinone: a novel cofactor.]]></article-title>
<source><![CDATA[Vitam Horm]]></source>
<year>1989</year>
<volume>45</volume>
<page-range>223-62</page-range></nlm-citation>
</ref>
<ref id="B5">
<label>5</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Houck]]></surname>
<given-names><![CDATA[D.R.]]></given-names>
</name>
<name>
<surname><![CDATA[Hanners]]></surname>
<given-names><![CDATA[J.L.]]></given-names>
</name>
<name>
<surname><![CDATA[Unkefer]]></surname>
<given-names><![CDATA[C.J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Biosynthesis of pyrroloquinoline quinone. Identification of biosynthetic precursors using 13C and NMR spectroscopy]]></article-title>
<source><![CDATA[J. Am. Chem. Soc.]]></source>
<year>1988</year>
<volume>110</volume>
<page-range>6920-1</page-range></nlm-citation>
</ref>
<ref id="B6">
<label>6</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Houck]]></surname>
<given-names><![CDATA[D.R.]]></given-names>
</name>
<name>
<surname><![CDATA[Hanners]]></surname>
<given-names><![CDATA[J.L.]]></given-names>
</name>
<name>
<surname><![CDATA[Unkefer]]></surname>
<given-names><![CDATA[C.J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Biosynthesis of pyrroloquinoline quinone 2. Biosynthetic assembly from glutamate and tyrosine]]></article-title>
<source><![CDATA[J. Am. Chem. Soc.]]></source>
<year>1991</year>
<volume>113</volume>
<page-range>3162-6</page-range></nlm-citation>
</ref>
<ref id="B7">
<label>7</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Meulenberg]]></surname>
<given-names><![CDATA[J.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Sellink]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
<name>
<surname><![CDATA[Riegman]]></surname>
<given-names><![CDATA[N.H.]]></given-names>
</name>
<name>
<surname><![CDATA[Postma]]></surname>
<given-names><![CDATA[P.Q]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Nucleotide sequence and structure of the Klebsiella pneumoniae pqq operon]]></article-title>
<source><![CDATA[Mol. Gen. Genet]]></source>
<year>1992</year>
<volume>232</volume>
<page-range>284-94</page-range></nlm-citation>
</ref>
<ref id="B8">
<label>8</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Mutzel]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Gorisch]]></surname>
<given-names><![CDATA[H]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Quinoprotein ethanol dehydrogenase preparation of the apo-form and reconstitution with pyrroloquinoline quinone and Ca2+ o Sr2+ ions]]></article-title>
<source><![CDATA[Agric. Bil. Chem]]></source>
<year>1991</year>
<volume>55</volume>
<page-range>1721-6</page-range></nlm-citation>
</ref>
<ref id="B9">
<label>9</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Itoh]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Kawakani]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Fukuzumi]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Modeling of the chemistry of quinoprotein methanol dehydogenase, oxidation of methanol by calcium complex of coenzyme PQQ via addition-elimination mechanism]]></article-title>
<source><![CDATA[J. Am. Chem. Soc]]></source>
<year>1997</year>
<volume>119</volume>
<page-range>439-40</page-range></nlm-citation>
</ref>
<ref id="B10">
<label>10</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Duine]]></surname>
<given-names><![CDATA[J.A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Quinoproteins-enzyme containing the cofactor pyrroloquinoline quinone, topaquinone or tryptophan quinone]]></article-title>
<source><![CDATA[Eur. J. Biochem]]></source>
<year>1991</year>
<volume>200</volume>
<page-range>271 284</page-range></nlm-citation>
</ref>
<ref id="B11">
<label>11</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Harris]]></surname>
<given-names><![CDATA[T.K.]]></given-names>
</name>
<name>
<surname><![CDATA[Davidson]]></surname>
<given-names><![CDATA[V.L]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Replacement of enzyme-bound calcium with strontium alters the kinetic properties of methanol dehydrogenase]]></article-title>
<source><![CDATA[Biochem, J]]></source>
<year>1994</year>
<volume>350</volume>
<page-range>917-23</page-range></nlm-citation>
</ref>
<ref id="B12">
<label>12</label><nlm-citation citation-type="book">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Anthony]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
</person-group>
<source><![CDATA[Principle and applications for quinoproteins]]></source>
<year>1993</year>
<page-range>50-68</page-range><publisher-loc><![CDATA[New York ]]></publisher-loc>
<publisher-name><![CDATA[Marcel Dekker]]></publisher-name>
</nlm-citation>
</ref>
<ref id="B13">
<label>13</label><nlm-citation citation-type="book">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Gorisch]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Rupp]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Quinoprotein ethanol dehydrogenase from Pseudomonas]]></article-title>
<person-group person-group-type="editor">
<name>
<surname><![CDATA[Jongejan]]></surname>
<given-names><![CDATA[J.A.]]></given-names>
</name>
<name>
<surname><![CDATA[Duine]]></surname>
<given-names><![CDATA[J.A]]></given-names>
</name>
</person-group>
<source><![CDATA[PQQ and quinoproteins]]></source>
<year>1989</year>
<page-range>23-34</page-range><publisher-loc><![CDATA[Dordreeth ]]></publisher-loc>
<publisher-name><![CDATA[Kluwer Academic Publishers]]></publisher-name>
</nlm-citation>
</ref>
<ref id="B14">
<label>14</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Toyama]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Three distinct quinoprotein alcohol dehydrogenase are expressed when Pseudomonas putida is grown on different alcohols]]></article-title>
<source><![CDATA[J. Bacteriol]]></source>
<year>1995</year>
<volume>177</volume>
<page-range>2442-50</page-range></nlm-citation>
</ref>
<ref id="B15">
<label>15</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Vangnai]]></surname>
<given-names><![CDATA[A.S.]]></given-names>
</name>
<name>
<surname><![CDATA[Arp]]></surname>
<given-names><![CDATA[D.J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[An inducible 1-butanol dehydrogenase, a quinohaemoprotein, is involved in the oxidation of butane by "Pseudomonas butanovora "]]></article-title>
<source><![CDATA[Microbiology]]></source>
<year>2001</year>
<volume>147</volume>
<page-range>745-56</page-range></nlm-citation>
</ref>
<ref id="B16">
<label>16</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Tachinaba]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<name>
<surname><![CDATA[Kuba]]></surname>
<given-names><![CDATA[N.]]></given-names>
</name>
<name>
<surname><![CDATA[Kawai]]></surname>
<given-names><![CDATA[F.]]></given-names>
</name>
<name>
<surname><![CDATA[Duine]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
<name>
<surname><![CDATA[Yasuda]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Involvement of a quinoprotein (PQQ-containig) alcohol dehydrogenase in the degradation of polypropylene glycols by the bacterium Stenotrophomonas maltophilia]]></article-title>
<source><![CDATA[FEMS Microbiolog Letters]]></source>
<year>2003</year>
<volume>128</volume>
<page-range>345-9</page-range></nlm-citation>
</ref>
<ref id="B17">
<label>17</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Asakura]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Hoshino]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Isolation and characterization of a new quinoprotein dehydrogenase, L-sorbose/L-sorbosone dehydrogenase]]></article-title>
<source><![CDATA[Biosci. Biotech Biochem]]></source>
<year>1999</year>
<volume>62</volume>
<page-range>469-78</page-range></nlm-citation>
</ref>
<ref id="B18">
<label>18</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Shibata]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Purification and characterization of a quinoprotein acohol dehydrogenase from Pseudogluconobacte saccharoketigenes IFO 14464]]></article-title>
<source><![CDATA[J. Biosic. Bioeng]]></source>
<year>2001</year>
<volume>92</volume>
<page-range>524-31</page-range></nlm-citation>
</ref>
<ref id="B19">
<label>19</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Sugisawa]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Hoshino]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Purification and properties of membrane-bound D-sorbitol dehydrogenase from Gluconobacter suboxydans IFO 3255]]></article-title>
<source><![CDATA[Biosci Biotechnol Biochem]]></source>
<year>2002</year>
<volume>66</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>57-64</page-range></nlm-citation>
</ref>
<ref id="B20">
<label>20</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Yamanaka]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Tsuyuki]]></surname>
<given-names><![CDATA[Y]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Purification and characterization of membrane-bound glycerol dehydrogenase (GLDH) of Gluconobacter species]]></article-title>
<source><![CDATA[Agric. Biol. Chem]]></source>
<year>1983</year>
<volume>47</volume>
<page-range>2173-83</page-range></nlm-citation>
</ref>
<ref id="B21">
<label>21</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[De Jong]]></surname>
<given-names><![CDATA[G.A.H.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni purification, characterization, and reconstitution of the apoenzyme with pyrroloquinoline quinone analogues]]></article-title>
<source><![CDATA[Eur. J. Biochem]]></source>
<year>1995</year>
<volume>230</volume>
<page-range>899-905</page-range></nlm-citation>
</ref>
<ref id="B22">
<label>22</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Shimao]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Ninomiya]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Kuno]]></surname>
<given-names><![CDATA[O.]]></given-names>
</name>
<name>
<surname><![CDATA[Kato]]></surname>
<given-names><![CDATA[N.]]></given-names>
</name>
<name>
<surname><![CDATA[Sakazawa]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Existence of a novel enzyme, pyrroloquinoline quinone-dependent polyvinyl alcohol dehydrogenase, in a bacterial symbiont, Pseudomonas sp. strain VM15C]]></article-title>
<source><![CDATA[Appl Environ Microbiol]]></source>
<year>1986</year>
<volume>51</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>268-75</page-range></nlm-citation>
</ref>
<ref id="B23">
<label>23</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Zarnt]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<name>
<surname><![CDATA[Schrader]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Andreesen]]></surname>
<given-names><![CDATA[J.R]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Catalytic and molecular properties of the quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase from Ralstonia eutropha strain Bo]]></article-title>
<source><![CDATA[J Bacteriol]]></source>
<year>2001</year>
<volume>183</volume>
<numero>6</numero>
<issue>6</issue>
<page-range>1954-60</page-range></nlm-citation>
</ref>
<ref id="B24">
<label>24</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Adachi]]></surname>
<given-names><![CDATA[O.]]></given-names>
</name>
<name>
<surname><![CDATA[Miyagawa]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
<name>
<surname><![CDATA[Shinagawa]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
<name>
<surname><![CDATA[Matsushita]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Ameyana]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Purification and characterization of particulate alcohol dehydrogenase from Acetobacter aceti]]></article-title>
<source><![CDATA[Agric. Biol. Chem]]></source>
<year>1978</year>
<volume>42</volume>
<numero>12</numero>
<issue>12</issue>
<page-range>2331-40</page-range></nlm-citation>
</ref>
<ref id="B25">
<label>25</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Kondo]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Beppu]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Horinuochi]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Clonign, sequencing, and the characterization of the gene enconding the smallest subunit of the three componentmembrane bound alcohol dehydrogenase from Acetobacter pasteurians]]></article-title>
<source><![CDATA[J. Bacteriol]]></source>
<year>1995</year>
<volume>177</volume>
<page-range>5048-55</page-range></nlm-citation>
</ref>
<ref id="B26">
<label>26</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Tayama]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Fukawa]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Okumura]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Kawamuri]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Beppu]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Purification and characterization ofmembrane-bound alcohol dehydogenase from Acetobacter polyoxogenes]]></article-title>
<source><![CDATA[Appl Microbiol. Biotechnol]]></source>
<year>1989</year>
<volume>32</volume>
<page-range>181-5</page-range></nlm-citation>
</ref>
<ref id="B27">
<label>27</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Matsushita]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Takahashi]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Takahashi]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Ameyama]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Adachi]]></surname>
<given-names><![CDATA[O]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Methanol and ethanol oxidase respiratory chains of the methylotrophic acetic acid bacterium, Acetobacter methanolicus]]></article-title>
<source><![CDATA[J Biochem]]></source>
<year>1992</year>
<volume>111</volume>
<numero>6</numero>
<issue>6</issue>
<page-range>739-47</page-range><publisher-loc><![CDATA[Tokyo ]]></publisher-loc>
</nlm-citation>
</ref>
<ref id="B28">
<label>28</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Matsushita]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Yakushi]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Toyama]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Shinagawa]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
<name>
<surname><![CDATA[Adachi]]></surname>
<given-names><![CDATA[O]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Function of multiple heme C moites in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase cytocrome c complex of Gluconobacter suboxydans]]></article-title>
<source><![CDATA[J.Biol. Chem]]></source>
<year>1996</year>
<volume>271</volume>
<page-range>4850-7</page-range></nlm-citation>
</ref>
<ref id="B29">
<label>29</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Hopper]]></surname>
<given-names><![CDATA[D.J.]]></given-names>
</name>
<name>
<surname><![CDATA[Rogozinski]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Redox potential of the haem group in the quinocytochrome, lupanine hydroxilase, an enzyme located in the periplasma of a Pseudomonas sp]]></article-title>
<source><![CDATA[Biochem Biophys Acta]]></source>
<year>1998</year>
<volume>1383</volume>
<page-range>160-4</page-range></nlm-citation>
</ref>
<ref id="B30">
<label>30</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Adachi]]></surname>
<given-names><![CDATA[O.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Characterization of quinohemoprotein amine dehydrogenase from Pseudomonas putida]]></article-title>
<source><![CDATA[Biosci. Biotechnol. Biochem]]></source>
<year>1998</year>
<volume>62</volume>
<page-range>469-78</page-range></nlm-citation>
</ref>
<ref id="B31">
<label>31</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Takagi]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Torimura]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Kawaguchi]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Kano]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Ikeda]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Biochemical and electrochemical characterization of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans]]></article-title>
<source><![CDATA[Biochemistry]]></source>
<year>1999</year>
<volume>38</volume>
<numero>21</numero>
<issue>21</issue>
<page-range>6935-42</page-range></nlm-citation>
</ref>
<ref id="B32">
<label>32</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Toyama]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Mathews]]></surname>
<given-names><![CDATA[F.S.]]></given-names>
</name>
<name>
<surname><![CDATA[Adachi]]></surname>
<given-names><![CDATA[O.]]></given-names>
</name>
<name>
<surname><![CDATA[Matsushita]]></surname>
<given-names><![CDATA[K]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology]]></article-title>
<source><![CDATA[Arch Biochem Biophys]]></source>
<year>2004</year>
<volume>428</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>10-21</page-range></nlm-citation>
</ref>
<ref id="B33">
<label>33</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Amaratunga]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Goodwing]]></surname>
<given-names><![CDATA[P.M.]]></given-names>
</name>
<name>
<surname><![CDATA[O'Connor]]></surname>
<given-names><![CDATA[D.C.]]></given-names>
</name>
<name>
<surname><![CDATA[Anthony]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The methanol oxidation genes mxaFJGIR(S)ACKLD in Methylobacterium extorquenses]]></article-title>
<source><![CDATA[FEMS Microbiol. Lett]]></source>
<year>1997</year>
<volume>146</volume>
<page-range>31-8</page-range></nlm-citation>
</ref>
<ref id="B34">
<label>34</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Anthony]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The bacterial oxidation of methane and methanol]]></article-title>
<source><![CDATA[Adv Microbial Physiol]]></source>
<year>1986</year>
<volume>27</volume>
<page-range>113-210</page-range></nlm-citation>
</ref>
<ref id="B35">
<label>35</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[De Jong]]></surname>
<given-names><![CDATA[G.A.H.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Characterization of the interaction between PQQ and heme C in the quinohaemoprotein ethanol dehydrogenase from Comamonas testosteroni]]></article-title>
<source><![CDATA[Biochesmistry]]></source>
<year>1995</year>
<volume>34</volume>
<page-range>9451-8</page-range></nlm-citation>
</ref>
<ref id="B36">
<label>36</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Kondo]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Horinouchi]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Characterization of the genes encoding the three component membrane bound alcohol dehydogenase from Gluconobacter suboxydans and their expression in Acetobacterpasteurians]]></article-title>
<source><![CDATA[Appl. Environ. Micorbiol]]></source>
<year>1997</year>
<volume>63</volume>
<page-range>1131-8</page-range></nlm-citation>
</ref>
<ref id="B37">
<label>37</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Inoue]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Cloning and sequencing of the gene enconding the 72-kilodalton dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti]]></article-title>
<source><![CDATA[J. Bacteriol]]></source>
<year>1989</year>
<volume>171</volume>
<page-range>3115-22</page-range></nlm-citation>
</ref>
<ref id="B38">
<label>38</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Inoue]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Nucleotide sequence of the gene encoding the 45-kilodalton subunit of alcohol dehydrogenase from Acetobacter aceti]]></article-title>
<source><![CDATA[J. Ferment. Bioeng]]></source>
<year>1992</year>
<volume>73</volume>
<page-range>419-24</page-range></nlm-citation>
</ref>
<ref id="B39">
<label>39</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Matsushita]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Tataki]]></surname>
<given-names><![CDATA[Y.]]></given-names>
</name>
<name>
<surname><![CDATA[Shinagawa]]></surname>
<given-names><![CDATA[E.]]></given-names>
</name>
<name>
<surname><![CDATA[Ameyana]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Adachi]]></surname>
<given-names><![CDATA[O]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Ethanol oxidase respiratory chain of acetic acid bacteria-reactivity with ubiquinona of pyrroloquinoline quinone-dependt alcohol dehydrogenase purified from Acetobacter aceti and Gluconobacter suboxydans]]></article-title>
<source><![CDATA[Biosci. Biotechnol. Biochem]]></source>
<year>1992</year>
<volume>56</volume>
<page-range>304-10</page-range></nlm-citation>
</ref>
<ref id="B40">
<label>40</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Matsushita]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Soluble andmembrane quinoprotein D-glucose dehydrogenase of Acinetobacter calcoaceticus: the binding process of PQQ to the apoenzymes]]></article-title>
<source><![CDATA[Biosci. Biotechnol. Biochem]]></source>
<year>1995</year>
<volume>59</volume>
<page-range>1548-55</page-range></nlm-citation>
</ref>
<ref id="B41">
<label>41</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Ghosh]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
<name>
<surname><![CDATA[Anthony]]></surname>
<given-names><![CDATA[C.]]></given-names>
</name>
<name>
<surname><![CDATA[Harlo]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Goodwing]]></surname>
<given-names><![CDATA[M.G.]]></given-names>
</name>
<name>
<surname><![CDATA[Blake]]></surname>
<given-names><![CDATA[C.C.F]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The refined structure of the quinoprotein methanol dehydrogenase from Mehylobacterium extorquenses at 1.94 Ao]]></article-title>
<source><![CDATA[Structure]]></source>
<year>1995</year>
<volume>3</volume>
<page-range>177-87</page-range></nlm-citation>
</ref>
<ref id="B42">
<label>42</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Keitel]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity]]></article-title>
<source><![CDATA[J Mol Biol]]></source>
<year>2000</year>
<volume>297</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>961-74</page-range></nlm-citation>
</ref>
<ref id="B43">
<label>43</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Oubrie]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
<name>
<surname><![CDATA[Rozeboom]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Halk.]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Huizinga]]></surname>
<given-names><![CDATA[G]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni]]></article-title>
<source><![CDATA[The Journal of Biological Biochemistry]]></source>
<year>2002</year>
<volume>277</volume>
<page-range>3727-32</page-range></nlm-citation>
</ref>
<ref id="B44">
<label>44</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Xia]]></surname>
<given-names><![CDATA[Z.X.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i]]></article-title>
<source><![CDATA[J Biol Inorg Chem]]></source>
<year>2003</year>
<volume>8</volume>
<numero>8</numero>
<issue>8</issue>
<page-range>843-54</page-range></nlm-citation>
</ref>
<ref id="B45">
<label>45</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Matsushita]]></surname>
<given-names><![CDATA[K.]]></given-names>
</name>
<name>
<surname><![CDATA[Yamashita]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
<name>
<surname><![CDATA[Aoki]]></surname>
<given-names><![CDATA[N.]]></given-names>
</name>
<name>
<surname><![CDATA[Toyama]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
<name>
<surname><![CDATA[Adachi]]></surname>
<given-names><![CDATA[O]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5]]></article-title>
<source><![CDATA[Biochemistry]]></source>
<year>1999</year>
<volume>38</volume>
<page-range>6111-8</page-range></nlm-citation>
</ref>
</ref-list>
</back>
</article>
