Dimers of nicotinamide adenine dinucleotide: New evidence for the structure and the involvement in an enzymatic redox process

Carelli, Vincenzo; Liberatore, Felice; Casini, Antonio; Mondelli, R.; Arnone, Alberto; Carelli, Italo; Rotilio, Giuseppe; Mavelli, Irene

doi:10.1016/0045-2068(80)90044-9

Cited by 34 publications

(17 citation statements)

References 17 publications

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“…A typical NMR spectrum of (NAD) 2 synthesized in‐house (Fig. 3a) corresponds closely to published spectra [28–32]. We have found traces of the dimer in several samples of the oscillatory reaction mixture (a typical case is shown in Fig.…”

Section: Resultssupporting

confidence: 75%

“…The simulation of (NAD) 2 reactivity with oxidized HRP supports oxidative cleavege. Reported one‐electron enzymatic oxidation of the (NAD) 2 [38] and observation of hydrogen peroxide production in reaction of (NAD) 2 with mitochondrial extracts [28] also support this inference.…”

Section: Discussionmentioning

confidence: 81%

“…Dimerization readily occurs in solutions upon generation of NAD · , yielding a mixture of dimers, mostly 4,4′ isomers in various configurations [28–32]. A typical NMR spectrum of (NAD) 2 synthesized in‐house (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The absorbance ratio ( A 258 nm / A 340 nm ) of final solutions ranged from 5.4 to 5.05. NMR tests detected (NAD) 2 [28], less than 5% of β‐NAD + , less than 1% of impurities, and no NADH. The product could be stored under N 2 in the dark at 4 °C without apparent change for at least one week.…”

Section: Methodsmentioning

confidence: 99%

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Nicotinamide adenine dinucleotide species in the horseradish peroxidase–oxidase oscillator

Kirkor

Scheeline

2000

European Journal of Biochemistry

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NADH chemistry ancillary to the oscillatory peroxidase±oxidase (PO) reaction has been reexamined. Previously, (NAD) 2 has been thought of as a terminal, inert product of the PO reaction. We now show that (NAD) 2 is a central reactant in this system. Although we found traces of the dimer after several hours of the PO reaction, no accumulation of the dimer occurred, regardless of the reaction time or the number of oscillations. (NAD Keywords: horseradish peroxidase catalysis; methylene blue; NAD anomers; NAD dimer; rate constants.Peroxidases are widely distributed floral, fungal and animal heme-containing enzymes. Across the phyla, this class of enzymes participates in oxidations and reductions essential in anti-infectious defenses, hormonal signaling, and in a plants' formation and maintenance of cell walls. In mammals, peroxidases are also implicated in the pathology of inflammation. Horseradish peroxidase has found wide-spread use in a multitude of analytical assays and biosensors [1]. Due to its wide-range of catalytic activity and ready availability, HRP serves as the archetypal peroxidase in investigations of mechanisms of biochemical redox reactions. Even more importantly, pyridine nucleotides are the most common coenzymes in plant and animal cellular metabolism. NADH (Fig. 1) is one of a few substrates that activates both oxidase and peroxidase cycles of peroxidases. In stimulated neutrophils, pyridine coenzymes serve as the source of electrons shuttled by NADH oxidase through the plasma membrane to oxygen, in formation of superoxide radicals and activation of antimicrobial defenses, the chlorinating system of myeloperoxidase among them. The main target of this work is an assessment of the role of (NAD) 2 (Fig. 1) in reaction pathways operating in the horseradish peroxidase-catalyzed oxidation of NADH. A secondary goal concerns establishing the roles of other b-NADH-derived species in the PO reaction. Explorations of reduced nicotinamide adenine dinucleotide (NADH) reaction pathways are notoriously difficult. The difficulty lies in the wide range of transformations and instability of intermediates that can form. It is manifest in a large number of model compounds synthesized to restrict possible transformations. We select the HRP-NADH-O 2 oscillator as, on one hand, a more stringent framework for mechanistic evaluation of the relevant chemistry of NADH, and on the other hand, a medium kinetically enforcing a hierarchy of reaction pathways [2]. The HRP-NADH-O 2 reaction is the most thoroughly studied in the group of peroxidase oscillators [3]. The abstract models of this oscillator emulate its observable PO dynamics with general fidelity. Chemically realistic models, however, have been found lacking in simulating several features of the oscillator [4]. Our current work increases the number of reactions demonstrated to occur in the PO oscillator.In aqueous solutions of moderate acidity, the main transformations of nicotinamide adenine dinucleotide are acidcatalyzed autooxidation, anomerization, and hydration...

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Section: Resultssupporting

confidence: 75%

Section: Discussionmentioning

confidence: 81%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Nicotinamide adenine dinucleotide species in the horseradish peroxidase–oxidase oscillator

Kirkor

Scheeline

2000

European Journal of Biochemistry

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“…[11][12][13][14][15][16] Furthermore, accumulation of oxidation products involving radical intermediates, such as dimer from the one-electron oxidation product NAD +. , 17,18 can cause deactivation and fouling of the electrode surface. Such contamination of the working electrode can largely lower the sensitivity and reproducibility of voltammetric measurements.…”

mentioning

confidence: 99%

Investigation of Direct Electrooxidation Behavior of NADH at a Chemically Modified Glassy Carbon Electrode

Jin

Peng

et al. 2015

J. Electrochem. Soc.

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In this study, the composite material that made up polyglycine/3d-4f hybrid-metallic cyano-bridged mixed coordination polymers (CyMCP) was successfully decorated onto a glassy carbon rotating disk electrode (GC RDE) using electrodeposition. The voltammetric behavior of NADH showed typical direct electrooxidation characteristics on the modified GC electrode. Our polyglycine/CyMCP-modified GC RDE was able to measure the apparent heterogeneous electron transfer rate constant of NADH during its direct electrooxidation by preventing fouling effects on the working electrode, which would generally cause a decrease in the oxidative peak current of NADH. In addition, differential pulse voltammetry provided a large linear range between the oxidative peak current and the concentration of NADH from 2-1500 μM at the polyglycine/CyMCP/GC electrode. Finally, the apparent heterogeneous electron transfer rate constant (k s NADH ) of NADH was determined to be 1.73 × 10 −2 cm · s −1 using the polyglycine/CyMCP-modified GC RDE. Both reduced and oxidized forms of β-nicotinamide adenine dinucleotide (NADH and NAD + , respectively) are the coenzymes for a large number of dehydrogenase enzymes (>300) and components of biomarker systems.1 In fact, because of its very important role in the field of analytical electrochemistry, 2,3 bioelectrocatalysis 4-6 and biofuel cells, 7,8 the electrochemical investigation for the formal potential of NADH/NAD + redox couple has attracted much attention. 9,10Therefore, direct oxidation of NADH at untreated or unmodified classical solid electrodes is known to appear poor reversibility and occurs with considerable overpotential (e.g., 1.1 V on carbon and 1.3 V on platinum). [11][12][13][14][15][16] Furthermore, accumulation of oxidation products involving radical intermediates, such as dimer from the one-electron oxidation product NAD +. , 17,18 can cause deactivation and fouling of the electrode surface. Such contamination of the working electrode can largely lower the sensitivity and reproducibility of voltammetric measurements. Consequently, considerable effort has been devoted with a strategy of surface modification on the substrate of conventional materials electrode to attain the electrode's long term stability for determination of NADH at a lower potential. 2,[19][20][21] Over the last few decades, various carbon nanomaterial 22-24 and redox-active mediator materials [25][26][27][28][29][30][31][32][33][34][35] have been modified onto the electrode surface in order to alleviate and/or prevent higher overpotential and fouling problems of the electrode. Therefore, there exist two kinds of catalytic model for the electrooxidation of NADH: one is a direct electro-catalysis 13,15,16,36 and the other is called a redox mediator electro-catalysis. [25][26][27][28][29][30][31][32]37 Though these redox mediators are very efficient electron shuttles for NADH oxidation processes, hydrodynamic voltammetry on the mediator-modified electrode remains a challenge for examining the kinetic parameters of NADH elect...

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Structure of the Dimers Obtained From the Reduction of 1-Benzyl-3,5-bis(dialkylcarbamoyl)pyridinium Ions – Models of NAD+

Leprêtre¹,

Limosin

Gérard³

et al. 1998

Eur. J. Org. Chem.

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Dimers of nicotinamide adenine dinucleotide: New evidence for the structure and the involvement in an enzymatic redox process

Cited by 34 publications

References 17 publications

Nicotinamide adenine dinucleotide species in the horseradish peroxidase–oxidase oscillator

Nicotinamide adenine dinucleotide species in the horseradish peroxidase–oxidase oscillator

Investigation of Direct Electrooxidation Behavior of NADH at a Chemically Modified Glassy Carbon Electrode

Structure of the Dimers Obtained From the Reduction of 1-Benzyl-3,5-bis(dialkylcarbamoyl)pyridinium Ions – Models of NAD+

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