Quinohemoprotein alcohol dehydrogenases: structure, function, and physiology

Toyama, Hirohide; Mathews, F.S.; Adachi, Osao; Matsushita, Kazunobu

doi:10.1016/j.abb.2004.03.037

Cited by 105 publications

(88 citation statements)

References 43 publications

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“…There are three types of PQQ-dependent dehydrogenases and the type II and type III are quinohaemoproteins containing both the PQQ cofactor and at least one haem. Type II are defined as soluble, periplasmic quinohaemoproteins and type III are membrane-bound quinohaemoproteins [82]. These dehydrogenases are similar to FAD-dependent dehydrogenases in that they do not include a diffusional cofactor and can use the haem-containing subunit as a relay to internally transfer electrons to/from the electrode.…”

mentioning

confidence: 99%

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Milton

Minteer

2017

J. R. Soc. Interface.

166

148

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Enzymatic bioelectrocatalysis is being increasingly exploited to better understand oxidoreductase enzymes, to develop minimalistic yet specific biosensor platforms, and to develop alternative energy conversion devices and bioelectrosynthetic devices for the production of energy and/or important chemical commodities. In some cases, these enzymes are able to electronically communicate with an appropriately designed electrode surface without the requirement of an electron mediator to shuttle electrons between the enzyme and electrode. This phenomenon has been termed direct electron transfer or direct bioelectrocatalysis. While many thorough studies have extensively investigated this fascinating feat, it is sometimes difficult to differentiate desirable enzymatic bioelectrocatalysis from electrocatalysis deriving from inactivated enzyme that may have also released its catalytic cofactor. This article will review direct bioelectrocatalysis of several oxidoreductases, with an emphasis on experiments that provide support for direct bioelectrocatalysis versus denatured enzyme or dissociated cofactor. Finally, this review will conclude with a series of proposed control experiments that could be adopted to discern successful direct electronic communication of an enzyme from its denatured counterpart.

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mentioning

confidence: 99%

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Milton

Minteer

2017

J. R. Soc. Interface.

166

148

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“…The partial adhA homolog from A. tropicalis NBRC16470 was similar to the adhA sequences from Acetobacter pasteurianus 16 and Acetobacter aceti 17 ; the sequence of the translated polypeptide was 86 identical to AdhA from A. pasteurianus and 85 identical to that from A. aceti. Usually, AdhA contains PQQ and one heme c, and the amino acid residues involved in both PQQ and heme c binding have been identified in ADH based on genetic and structural information 18 . Within the sequenced region of the AdhA homolog, amino acid residues involved in PQQ binding were also identifi ed alignment not shown .…”

Section: Resultsmentioning

confidence: 99%

Membrane-Bound Alcohol Dehydrogenase Is Essential for Glyceric Acid Production in Acetobacter tropicalis

Habe¹,

Sato²,

Fukuoka³

et al. 2011

J. Oleo Sci.

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“…Se-Met labeled XcPqqD was prepared in a similar way, and was produced using an E. coli strain BL21 (DE3) as the host in the absence of methionine, but in the presence of large amounts of Se-Met (100 mg/L). The M9 minimum medium consists of 1 g of NH 4 Cl, 3 g of KH 2 PO 4 , and 6 g of Na 2 HPO 4 , 0.3% (w/v) of MgSO 4 , and 10 mg of FeSO 4 in one liter of double-distilled water supplemented with 20% (w/v) of glucose. The induction was conducted at 293 K for 20 hours by the addition of 0.5 mM IPTG.…”

Section: Methodsmentioning

confidence: 99%