The Silent Form of Quinohemoprotein Amine Dehydrogenase from<i>Paracoccus denitrificans</i>

Fujieda, Nobutaka; Mori, Megumi; Ikeda, Tokuji; Kano, Kenji

doi:10.1271/bbb.80578

Cited by 4 publications

(3 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is also noteworthy that the γ subunit produced by PdΔqhpG cells gives only a single band on a Western blot, whereas the periplasmic fractions of wild-type Pd1222 and plasmid-rescued mutant strains show multiple (apparently three) bands for the γ subunit on a stained blot, although quinone detection reveals only one band. Fujieda et al reported that a silent (inactive) form of QHNDH was produced alongside active enzyme in P. denitrificans grown in a medium containing n -butylamine . The silent form of QHNDH was shown to contain an oxime (C6NOH) of CTQ, which may be formed by reaction with hydroxylamine in the cells and can be slowly reactivated by incubation with amine substrates.…”

Section: Resultsmentioning

confidence: 99%

“…Fujieda et al reported that a silent (inactive) form of QHNDH was produced alongside active enzyme in P. denitrificans grown in a medium containing n-butylamine. 32 The silent form of QHNDH was shown to contain an oxime (C6NOH) of CTQ, which may be formed by reaction with hydroxylamine in the cells and can be slowly reactivated by incubation with amine substrates. It is therefore very likely that the multiple γ subunit bands shown by Western blot analysis can be explained, at least in part, by the presence of the γ subunit containing the CTQ-oxime, which is presumably formed after the biogenesis of active QHNDH has been completed in the periplasm.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Identification of Genes Essential for the Biogenesis of Quinohemoprotein Amine Dehydrogenase

et al. 2014

View full text Add to dashboard Cite

The structural genes encoding quinohemoprotein amine dehydrogenase (QHNDH) in Gram-negative bacteria constitute a polycistronic operon together with several nearby genes, which are collectively termed "qhp". We previously showed that the qhpD gene, which lies between qhpA and qhpC (encoding the α and γ subunits of QHNDH, respectively), and the qhpE gene, which follows qhpB (encoding the β subunit), both encode enzymes specifically involved in the posttranslational modification of the γ subunit and are hence essential for QHNDH biogenesis in Paracoccus denitrificans [Ono, K., et al. (2006) J. Biol. Chem. 281, 13672-13684; Nakai, T., et al. (2012) J. Biol. Chem. 287, 6530-6538]. Here we further demonstrate that the qhpF gene, which follows qhpE, and the qhpG and qhpR genes, peripherally located in the complementary strand, are also indispensable for QHNDH biogenesis. The qhpF gene encodes an efflux ABC transporter, which probably translocates the γ subunit into the periplasm in a process coupled with hydrolysis of ATP. The qhpG gene encodes a putative FAD-dependent monooxygenase, which is required for the generation of the quinone cofactor in the γ subunit. Finally, the qhpR gene encodes an AraC family transcriptional regulator, which activates expression of the qhp operon in response to the addition of n-butylamine to the culture medium. Database analysis of the qhp genes reveals that they are very widely distributed, not only in many Gram-negative species but also in a few Gram-positive bacteria.

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Identification of Genes Essential for the Biogenesis of Quinohemoprotein Amine Dehydrogenase

et al. 2014

View full text Add to dashboard Cite

show abstract

“…n-butylamine, methylamine, histamine) to aldehyde and ammonia, allowing organism growth using amines as the sole source of carbon and energy. The enzyme has two heme c groups and a quinone as cofactors in its heterotrimeric structure [77].…”

Section: Cytochrome C550mentioning

confidence: 99%

Small electron-transfer proteins as mediators in enzymatic electrochemical biosensors

Silveira

Almeida

2013

Anal Bioanal Chem

View full text Add to dashboard Cite

Electrochemical mediators transfer redox equivalents between the active sites of enzymes and electrodes and, in this way, trigger bioelectrocatalytic redox processes. This has been very useful in the development of the so-called second generation biosensors, where they are able to transduce the catalytic event into an electrical signal. Among other pre-requisites, redox mediators must be readily oxidized/reduced at the electrode surface and easily interact with the biorecognition component. Small chemical compounds (e.g. ferrocene derivatives, ruthenium or osmium complexes and viologens) are frequently used for this purpose, but lately, small redox proteins (e.g. horse heart cytochrome c) have also played the role of redox partners in biosensing applications. In general, the docking between two complementary proteins introduces a second level of selectivity to the biosensor and enlarges the list of compounds targeted for analysis. Moreover, electrochemical interferences are frequently minimized owing to the small overpotentials achieved. This paper aims to provide an overview of enzyme biosensors that are mediated by electron transfer proteins. The article begins with a few considerations on mediated electrochemistry in biosensing 2 systems and proceeds with a detailed description of relevant works concerning the cooperative use of redox enzymes and biological electron donors/acceptors.

show abstract

Redox Proteins and Bioelectrocatalysis

Kano

Shirai

Kitazumi

et al. 2020

Enzymatic Bioelectrocatalysis

View full text Add to dashboard Cite

The Silent Form of Quinohemoprotein Amine Dehydrogenase fromParacoccus denitrificans

Cited by 4 publications

References 27 publications

Identification of Genes Essential for the Biogenesis of Quinohemoprotein Amine Dehydrogenase

Identification of Genes Essential for the Biogenesis of Quinohemoprotein Amine Dehydrogenase

Small electron-transfer proteins as mediators in enzymatic electrochemical biosensors

Redox Proteins and Bioelectrocatalysis

Contact Info

Product

Resources

About