Prosthetic Group of Aldehyde Dehydrogenase in Acetic Acid Bacteria Not Pyrroloquinoline Quinone

1994 ◽  
Vol 58 (11) ◽  
pp. 2082-2083 ◽  
Author(s):  
Hiroshi Takemura ◽  
Takayasu Tsuchida ◽  
Fumihiro Yoshinaga ◽  
Kazunobu Matsushita ◽  
Osao Adachi
Keyword(s):  
Acetic Acid ◽  
Aldehyde Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Pyrroloquinoline Quinone ◽  
Prosthetic Group

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 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 Reversible thermal inactivation of the quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus. Ca2+ ions are necessary for re-activation

1989 ◽  
Vol 261 (2) ◽  
pp. 415-421 ◽  
Author(s):  
O Geiger ◽  
H Görisch
Keyword(s):  
Acetic Acid ◽  
Active Site ◽  
Protein Concentration ◽  
Thermal Inactivation ◽  
Glucose Dehydrogenase ◽  
Acinetobacter Calcoaceticus ◽  
Pyrroloquinoline Quinone ◽  
Soluble Form ◽  
Activation Process ◽  
Prosthetic Group

The soluble form of the homogeneous quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus is reversibly inactivated at temperatures above 35 degrees C. An equilibrium is established between active and denatured enzyme, this depending on the protein concentration and the inactivation temperature used. Upon thermal inactivation the enzyme dissociates into the prosthetic group pyrroloquinoline quinone and the apo form of glucose dehydrogenase. After inactivation at 50 degrees C active enzyme is re-formed again at 25 degrees C. Ca2+ ions are necessary for the re-activation process. The velocity of re-activation depends on the protein concentration, the concentration of the prosthetic group pyrroloquinoline quinone and the Ca2+ concentration. The apo form of glucose dehydrogenase can be isolated, and in the presence of pyrroloquinoline quinone and Ca2+ active holoenzyme is formed. Even though native glucose dehydrogenase is not inactivated in the presence of EDTA or trans-1,2-diaminocyclohexane-NNN'NH-tetra-acetic acid, Ca2+ stabilizes the enzyme against thermal inactivation. Two Ca2+ ions are found per subunit of glucose dehydrogenase. The data suggest that pyrroloquinoline quinone is bound at the active site via a Ca2+ bridge. Mn2+ and Cd2+ can replace Ca2+ in the re-activation mixture.

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