scholarly journals The inactive and active forms of the pyrroloquinoline quinone-alcohol dehydrogenase of Gluconacetobacter diazotrophicus: a comparative study

2013 ◽  
Vol 2 (1s) ◽  
pp. 2 ◽  
Author(s):  
Saul Gomez-Manzo ◽  
Irene Patricia Del Arenal-Mena ◽  
Edgardo Escamilla
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Comparative Study ◽  
Redox State ◽  
Catalytic Properties ◽  
Acetic Acid Bacteria ◽  
Pyrroloquinoline Quinone ◽  
Gluconacetobacter Diazotrophicus ◽  
Membrane Bound ◽  
Prosthetic Groups

<em>Gluconacetobacter diazotrophicus</em> as a member of the acetic acid bacteria group, oxidize alcohol to acetic acid through two sequential reactions catalyzed by the alcohol dehydrogenase (ADH) and the aldehyde dehydrogenase, both enzymes are membrane-bound and oriented to the periplasmic space. ADH is a quinohemoprotein carrying one pyrroloquinoline quinone moiety, one [2Fe:2S] cluster and four c-type cytochromes, as prosthetic groups. In recent years has been described the presence of the inactive ADH (ADHi) in the acetic acid bacteria. In the present review we make a comparative study of the molecular and catalytic properties of the active and inactive forms of ADH purified from <em>G. diazotrophicus</em>, variation in the redox state of enzymes <em>as purified </em>could explain the notorious differences seen in the activity power of the compared enzymes.

scholarly journals Molecular and Catalytic Properties of the Aldehyde Dehydrogenase of Gluconacetobacter diazotrophicus, a Quinoheme Protein Containing Pyrroloquinoline Quinone, Cytochrome b, and Cytochrome c

2010 ◽  
Vol 192 (21) ◽  
pp. 5718-5724 ◽  
Author(s):  
S. Gómez-Manzo ◽  
J. L. Chavez-Pacheco ◽  
M. Contreras-Zentella ◽  
M. E. Sosa-Torres ◽  
R. Arreguín-Espinosa ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Aldehyde Dehydrogenase ◽  
Catalytic Properties ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Acetic Acid Bacteria ◽  
Pyrroloquinoline Quinone ◽  
Reversed Phase ◽  
Resonance Spectroscopy ◽  
Gluconacetobacter Diazotrophicus ◽  
Vis Spectroscopy

ABSTRACT Several aldehyde dehydrogenase (ALDH) complexes have been purified from the membranes of acetic acid bacteria. The enzyme structures and the chemical nature of the prosthetic groups associated with these enzymes remain a matter of debate. We report here on the molecular and catalytic properties of the membrane-bound ALDH complex of the diazotrophic bacterium Gluconacetobacter diazotrophicus. The purified ALDH complex is a heterodimer comprising two subunits of 79.7 and 50 kDa, respectively. Reversed-phase high-pressure liquid chromatography (HPLC) and electron paramagnetic resonance spectroscopy led us to demonstrate, for the first time, the unequivocal presence of a pyrroloquinoline quinone prosthetic group associated with an ALDH complex from acetic acid bacteria. In addition, heme b was detected by UV-visible light (UV-Vis) spectroscopy and confirmed by reversed-phase HPLC. The smaller subunit bears three cytochromes c. Aliphatic aldehydes, but not formaldehyde, were suitable substrates. Using ferricyanide as an electron acceptor, the enzyme showed an optimum pH of 3.5 that shifted to pH 7.0 when phenazine methosulfate plus 2,6-dichlorophenolindophenol were the electron acceptors. Acetaldehyde did not reduce measurable levels of the cytochrome b and c centers; however, the dithionite-reduced hemes were conveniently oxidized by ubiquinone-1; this finding suggests that cytochrome b and the cytochromes c constitute an intramolecular redox sequence that delivers electrons to the membrane ubiquinone.

scholarly journals The active (ADHa) and inactive (ADHi) forms of the PQQ-alcohol dehydrogenase from Gluconacetobacter diazotrophicus differ in their respective oligomeric structures and redox state of their corresponding prosthetic groups

2012 ◽  
Vol 328 (2) ◽  
pp. 106-113 ◽  
Author(s):  
Saúl Gómez-Manzo ◽  
Alejandra Abigail González-Valdez ◽  
Jesús Oria-Hernández ◽  
Horacio Reyes-Vivas ◽  
Roberto Arreguín-Espinosa ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Redox State ◽  
Gluconacetobacter Diazotrophicus ◽  
Prosthetic Groups

scholarly journals Crystallization of Membrane-bound Alcohol Dehydrogenase of Acetic Acid Bacteria

1982 ◽  
Vol 46 (11) ◽  
pp. 2859-2863
Author(s):  
Osao Adachi ◽  
Emiko Shinagawa ◽  
Kazunobu Matsushita ◽  
Minoru Ameyama
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Membrane Bound

scholarly journals Crystallization of membrane-bound alcohol dehydrogenase of acetic acid bacteria.

1982 ◽  
Vol 46 (11) ◽  
pp. 2859-2863 ◽  
Author(s):  
Osao ADACHI ◽  
Emiko SHINAGAWA ◽  
Kazunobu MATSUSHITA ◽  
Minoru AMEYAMA
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Membrane Bound

Identifying membrane-bound quinoprotein glucose dehydrogenase from acetic acid bacteria that produce lactobionic and cellobionic acids

2019 ◽  
Vol 83 (6) ◽  
pp. 1171-1179 ◽  
Author(s):  
Takaaki Kiryu ◽  
Taro Kiso ◽  
Daisuke Koma ◽  
Shigemitsu Tanaka ◽  
Hiromi Murakami
Keyword(s):  
Acetic Acid ◽  
Glucose Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Membrane Bound

scholarly journals Formation of 4-Keto-D-aldopentoses and 4-Pentulosonates (4-Keto-D-pentonates) with Unidentified Membrane-Bound Enzymes from Acetic Acid Bacteria

2011 ◽  
Vol 75 (9) ◽  
pp. 1801-1806 ◽  
Author(s):  
Osao ADACHI ◽  
Roque A. HOURS ◽  
Emiko SHINAGAWA ◽  
Yoshihiko AKAKABE ◽  
Toshiharu YAKUSHI ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Acetic Acid Bacteria ◽  
Membrane Bound ◽  
Membrane Bound Enzymes
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