Evidence for a membrane-bound pyrroloquinoline quinone-linked glucose dehydrogenase in Acetobacter diazotrophicus

1995 ◽  
Vol 43 (4) ◽  
pp. 713-716 ◽  
Author(s):  
M. L. Galar ◽  
J. L. Boiardi
1995 ◽  
Vol 61 (5) ◽  
pp. 2069-2069
Author(s):  
M Shinjoh ◽  
N Tomiyama ◽  
A Asakura ◽  
T Hoshino

Volume 61, no. 2, p. 419, column 1, lines 15-19: this sentence should read as follows. "The alcohol dehydrogenase and glucose dehydrogenase have a common region reported to be related to pyrroloquinoline quinone binding (2, 10), but SNDH does not contain such a region, indicating that SNDH is not a quinoprotein." Page 419, column 2, line 12: "(Table 4)" should read "(Table 3)." [This corrects the article on p. 413 in vol. 61.].


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Alexa M. Schmitz ◽  
Brooke Pian ◽  
Sean Medin ◽  
Matthew C. Reid ◽  
Mingming Wu ◽  
...  

AbstractBioleaching of rare earth elements (REEs), using microorganisms such as Gluconobacter oxydans, offers a sustainable alternative to environmentally harmful thermochemical extraction, but is currently not very efficient. Here, we generate a whole-genome knockout collection of single-gene transposon disruption mutants for G. oxydans B58, to identify genes affecting the efficacy of REE bioleaching. We find 304 genes whose disruption alters the production of acidic biolixiviant. Disruption of genes underlying synthesis of the cofactor pyrroloquinoline quinone (PQQ) and the PQQ-dependent membrane-bound glucose dehydrogenase nearly eliminates bioleaching. Disruption of phosphate-specific transport system genes enhances bioleaching by up to 18%. Our results provide a comprehensive roadmap for engineering the genome of G. oxydans to further increase its bioleaching efficiency.


2019 ◽  
Vol 83 (6) ◽  
pp. 1171-1179 ◽  
Author(s):  
Takaaki Kiryu ◽  
Taro Kiso ◽  
Daisuke Koma ◽  
Shigemitsu Tanaka ◽  
Hiromi Murakami

2013 ◽  
Vol 14 (12) ◽  
pp. 23244-23256 ◽  
Author(s):  
Koichi Abe ◽  
Wataru Yoshida ◽  
Kotaro Terada ◽  
Yukiko Yagi-Ishii ◽  
Stefano Ferri ◽  
...  

2008 ◽  
Vol 313 (1-2) ◽  
pp. 217-225 ◽  
Author(s):  
Cecilia E. Bernardelli ◽  
María F. Luna ◽  
María L. Galar ◽  
José L. Boiardi

2006 ◽  
Vol 188 (21) ◽  
pp. 7668-7676 ◽  
Author(s):  
Tina Hölscher ◽  
Helmut Görisch

ABSTRACT In Gluconobacter oxydans, pyrroloquinoline quinone (PQQ) serves as the cofactor for various membrane-bound dehydrogenases that oxidize sugars and alcohols in the periplasm. Proteins for the biosynthesis of PQQ are encoded by the pqqABCDE gene cluster. Our reverse transcription-PCR and promoter analysis data indicated that the pqqA promoter represents the only promoter within the pqqABCDE cluster of G. oxydans 621H. PQQ overproduction in G. oxydans was achieved by transformation with the plasmid-carried pqqA gene or the complete pqqABCDE cluster. A G. oxydans mutant unable to produce PQQ was obtained by site-directed disruption of the pqqA gene. In contrast to the wild-type strain, the pqqA mutant did not grow with d-mannitol, d-glucose, or glycerol as the sole energy source, showing that in G. oxydans 621H, PQQ is essential for growth with these substrates. Growth of the pqqA mutant, however, was found with d-gluconate as the energy source. The growth behavior of the pqqA mutant correlated with the presence or absence of the respective PQQ-dependent membrane-bound dehydrogenase activities, demonstrating the vital role of these enzymes in G. oxydans metabolism. A different PQQ-deficient mutant was generated by Tn5 transposon mutagenesis. This mutant showed a defect in a gene with high homology to the Escherichia coli tldD gene, which encodes a peptidase. Our results indicate that the tldD gene in G. oxydans 621H is involved in PQQ biosynthesis, possibly with a similar function to that of the pqqF genes found in other PQQ-synthesizing bacteria.


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