Function of multiple heme C moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome C complex of acetic acid bacteria

1997 ◽  
Vol 67 (1-4) ◽  
pp. 137
Author(s):  
K. Matsushita ◽  
J. Frébortová ◽  
T. Yoshikawa ◽  
H. Toyama ◽  
O. Adachi
Keyword(s):  
Acetic Acid ◽  
Electron Transport ◽  
Cytochrome C ◽  
Alcohol Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
C Complex

scholarly journals A New Enzymatic Microdetermination Procedure for Ethanol with Particulate Alcohol Dehydrogenase from Acetic Acid Bacteria

1978 ◽  
Vol 42 (11) ◽  
pp. 2063-2069 ◽  
Author(s):  
Minoru Ameyama ◽  
Kenji Tayama ◽  
Eiji Miyagawa ◽  
Emiko Shinagawa ◽  
Kazunobu Matsushita ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Acetic Acid Bacteria

scholarly journals Replacement of a terminal cytochrome c oxidase by ubiquinol oxidase during the evolution of acetic acid bacteria

2014 ◽  
Vol 1837 (10) ◽  
pp. 1810-1820 ◽  
Author(s):  
Minenosuke Matsutani ◽  
Kota Fukushima ◽  
Chiho Kayama ◽  
Misato Arimitsu ◽  
Hideki Hirakawa ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Acetic Acid Bacteria ◽  
Ubiquinol Oxidase

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 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
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