Cyanide sensitivity in direct electron transfer-type bioelectrocatalysis by membrane-bound alcohol dehydrogenase from Gluconobacter oxydans

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.].

Download Full-text

X-ray structure of the direct electron transfer-type FAD glucose dehydrogenase catalytic subunit complexed with a hitchhiker protein

Acta Crystallographica Section D Structural Biology ◽

10.1107/s2059798319010878 ◽

2019 ◽

Vol 75 (9) ◽

pp. 841-851 ◽

Cited By ~ 3

Author(s):

Hiromi Yoshida ◽

Katsuhiro Kojima ◽

Masaki Shiota ◽

Keiichi Yoshimatsu ◽

Tomohiko Yamazaki ◽

...

Keyword(s):

Electron Transfer ◽

Disulfide Bonds ◽

Hydrophobic Interactions ◽

Direct Electron Transfer ◽

Glucose Dehydrogenase ◽

Catalytic Subunit ◽

Effective Electron ◽

Α Subunit ◽

X Ray ◽

Membrane Bound

The bacterial flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase complex derived from Burkholderia cepacia (BcGDH) is a representative molecule of direct electron transfer-type FAD-dependent dehydrogenase complexes. In this study, the X-ray structure of BcGDHγα, the catalytic subunit (α-subunit) of BcGDH complexed with a hitchhiker protein (γ-subunit), was determined. The most prominent feature of this enzyme is the presence of the 3Fe–4S cluster, which is located at the surface of the catalytic subunit and functions in intramolecular and intermolecular electron transfer from FAD to the electron-transfer subunit. The structure of the complex revealed that these two molecules are connected through disulfide bonds and hydrophobic interactions, and that the formation of disulfide bonds is required to stabilize the catalytic subunit. The structure of the complex revealed the putative position of the electron-transfer subunit. A comparison of the structures of BcGDHγα and membrane-bound fumarate reductases suggested that the whole BcGDH complex, which also includes the membrane-bound β-subunit containing three heme c moieties, may form a similar overall structure to fumarate reductases, thus accomplishing effective electron transfer.

Download Full-text

Bioanode with alcohol dehydrogenase undergoing a direct electron transfer on functionalized gold nanoparticles for an application in biofuel cells for glycerol conversion

Biosensors and Bioelectronics ◽

10.1016/j.bios.2017.06.048 ◽

2017 ◽

Vol 98 ◽

pp. 215-221 ◽

Cited By ~ 13

Author(s):

D. Ratautas ◽

L. Tetianec ◽

L. Marcinkevičienė ◽

R. Meškys ◽

J. Kulys

Keyword(s):

Gold Nanoparticles ◽

Electron Transfer ◽

Alcohol Dehydrogenase ◽

Direct Electron Transfer ◽

Biofuel Cells ◽

Glycerol Conversion ◽

Functionalized Gold Nanoparticles

Download Full-text

The First Step in Polyethylene Glycol Degradation by Sphingomonads Proceeds via a Flavoprotein Alcohol Dehydrogenase Containing Flavin Adenine Dinucleotide

Journal of Bacteriology ◽

10.1128/jb.183.22.6694-6698.2001 ◽

2001 ◽

Vol 183 (22) ◽

pp. 6694-6698 ◽

Cited By ~ 37

Author(s):

Manabu Sugimoto ◽

Miwa Tanabe ◽

Misako Hataya ◽

Shogo Enokibara ◽

Johannis A. Duine ◽

...

Keyword(s):

Alcohol Dehydrogenase ◽

Flavin Adenine Dinucleotide ◽

Gluconobacter Oxydans ◽

Gene Encoding ◽

E Coli ◽

Choline Dehydrogenase ◽

Nitrobenzyl Alcohol ◽

A Subunit ◽

Broad Variety ◽

Membrane Bound

ABSTRACT Several Sphingomonas spp. utilize polyethylene glycols (PEGs) as a sole carbon and energy source, oxidative PEG degradation being initiated by a dye-linked dehydrogenase (PEG-DH) that oxidizes the terminal alcohol groups of the polymer chain. Purification and characterization of PEG-DH from Sphingomonas terraerevealed that the enzyme is membrane bound. The gene encoding this enzyme (pegA) was cloned, sequenced, and expressed inEscherichia coli. The purified recombinant enzyme was vulnerable to aggregation and inactivation, but this could be prevented by addition of detergent. It is as a homodimeric protein with a subunit molecular mass of 58.8 kDa, each subunit containing 1 noncovalently bound flavin adenine dinucleotide but not Fe or Zn. PEG-DH recognizes a broad variety of primary aliphatic and aromatic alcohols as substrates. Comparison with known sequences revealed that PEG-DH belongs to the group of glucose-methanol-choline (GMC) flavoprotein oxidoreductases and that it is a novel type of flavoprotein alcohol dehydrogenase related (percent identical amino acids) to other, so far uncharacterized bacterial, membrane-bound, dye-linked dehydrogenases: alcohol dehydrogenase from Pseudomonas oleovorans(46%); choline dehydrogenase from E. coli (40%);l-sorbose dehydrogenase from Gluconobacter oxydans (38%); and 4-nitrobenzyl alcohol dehydrogenase from aPseudomonas species (35%).

Download Full-text