Non-enzymatic Interactions of Reduced Coenzyme I with Inorganic Phosphate and Certain Other Anions

Alivisatos, Spyridon G.A.; Ungar, Frieda; Abraham, George J.

doi:10.1038/203973a0

Cited by 36 publications

(27 citation statements)

References 7 publications

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“…10,11 Subsequently, for a correct description of the reaction progress over a longer time period, the spontaneous, irreversible decomposition of the cofactor NADH over time was included in the kinetic model. Assuming first-order kinetics as determined by Alivisatos et al 29 and Chenault and Whitesides 30 results in…”

Section: Mechanistic Kinetic Modelmentioning

confidence: 98%

“…The experiments reported here were performed at a 0.5 units higher pH and a twice as high buffer capacity. According to Alivisatos et al, 29 the resulting increase of H 2 PO À 4 concentration causes a decrease of NADH stability. In contrast, the negative slope of the progress curve cannot be explained by a proceeding deactivation of FDH.…”

Section: Prediction Of Reaction Coursesmentioning

confidence: 99%

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Mechanistic model for prediction of formate dehydrogenase kinetics under industrially relevant conditions

Schmidt

Michalik

Zavrel

et al. 2009

Biotechnology Progress

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Formate dehydrogenase (FDH) from Candida boidinii is an important biocatalyst for the regeneration of the cofactor NADH in industrial enzyme-catalyzed reductions. The mathematical model that is currently applied to predict progress curves during (semi-)batch reactions has been derived from initial rate studies. Here, it is demonstrated that such extrapolation from initial reaction rates to performance during a complete batch leads to considerable prediction errors. This observation can be attributed to an invalid simplification during the development of the literature model. A novel mechanistic model that describes the course and performance of FDH-catalyzed NADH regeneration under industrially relevant process conditions is introduced and evaluated. Based on progress curve instead of initial reaction rate measurements, it was discriminated from a comprehensive set of mechanistic model candidates. For the prediction of reaction courses on long time horizons (>1 h), decomposition of NADH has to be considered. The model accurately describes the regeneration reaction under all conditions, even at high concentrations of the substrate formate and thus is clearly superior to the existing model. As a result, for the first time, course and performance of NADH regeneration in industrial enzyme-catalyzed reductions can be accurately predicted and used to optimize the cost efficiency of the respective processes.

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Section: Mechanistic Kinetic Modelmentioning

confidence: 98%

Section: Prediction Of Reaction Coursesmentioning

confidence: 99%

Mechanistic model for prediction of formate dehydrogenase kinetics under industrially relevant conditions

Schmidt

Michalik

Zavrel

et al. 2009

Biotechnology Progress

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show abstract

“…Besides good reproducibility of the results, those authors observed a curvature in log-log current applied potential plots for potentials higher than 0.9 V and small decreases in currents across the transport limited region for replicate scans within a day by using steady-state voltammetry. These experimental observations were attributed to an eventual instability of NADH in phosphate buffer solution 9 and are also indicative of electrode poisoning. Experiments performed with nicotinamide mononucleotide (NMN + ) and its reduction product, NMNH, without adenine in the molecule, showed that adsorption on the electrode surfaces decreased 10 .…”

Section: Introductionmentioning

confidence: 99%

“…At pH 7.0, oxidation of adenine occurs at 0.9 V (vs SCE) 13 and a strong adsorption of the oxidation products has been reported 14 . From this viewpoint, the curvature in log-log current applied potential plots 4 could be due to oxidation of free adenine, coming from NADH -phosphate adducts decomposition 9 . In fact, electrochemical oxidation of NADH at a bare glassy carbon electrode was observed to be dependent on the supporting electrolyte composition.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of 3,4-dihydroxybenzaldehyde electropolymerization at carbon paste electrodes: catalytic detection of NADH

Delbem¹,

Baader²,

Serrano³

2002

Quím. Nova

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. Professsor Lineu Prestes, 748, 05508-900 São Paulo -SP Recebido em 26/5/01; aceito em 20/12/01Cyclic voltammetry was used to study 3,4-dihydroxybenzaldehyde (3,4-DHB) electropolymerization processes on carbon paste electrodes. The characteristics of the electropolymerized films were highly dependent on pH, anodic switching potential, scan rate, 3,4-DHB concentrations and number of cycles. Film stability was determined in citrate/phosphate buffer solutions at the same pH used during the electropolymerization process. The best conditions to prepare carbon paste modified electrodes were pH 7.8; 0.0 £ E apl £ 0.25 V; 10 mV s -1 ; 0.25 mmol L -1 3,4-DHB and 10 scans. These carbon paste modified electrodes were used for NADH catalytic detection at 0.23 V in the range 0.015 £ [NADH] £ 0.21 mmol L -1 . Experimental data were used to propose a mechanism for the 3,4-DHB electropolymerization processes, which involves initial phenoxyl radical formation.

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“…Zur Verbesserung der Stabilität wurde der Einfluß verschiedener Puffersysteme, des pH-Wertes der NADH-Lösung, von Anionen tirid Kationen sowie der NADH-Konzentration bei einzelnen Lagertemperaturen untersucht (1)(2)(3)(4)(5)(6)(7)(8), Dabei haben sich folgende Bedingungen als vorteilhaft erwiesen: 10 mmol/1 NADH in 50 mmol/1 Tris-EDTA-HCl, pH 7,7. Unter diesen Bedingungen ist das-NADH bei Raumtemperatur l Tag, und bei 2-8°C l Woche stabil ( Nachdem weitere Vorversuche zeigten, daß die Aktivitäts-bestimmung diagnostisch wichtiger Enzyme (LactatJDehydrogenase-1-Isoenzym, Glutamat-Dehydrogenase, Glutamat-Pyruvat-und Glutämat-Oxalacetat-Transaminase und Creatin-Kinase) durch das Lösungsmittel Ethylenglykol-50 mmol/1 Tris in der fraglichen Konzentration (bis 0,1 ml/2,7 ml Testlösung) nicht beeinflußt wird, wurde für die weiteren Versuche dieses Lösungsmittel eingesetzt.…”

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Stabilisierung des reduzierten β-Nicotinamid-Adenin-Dinucleotid in einem organischen Lösungsmittel

Gallati¹

1976

Clinical Chemistry and Laboratory Medicine

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Zusammenfassung: Das NADH zeigt eine erstaunlich gute Lagerstabilität, sofern dieses Coenzym nicht in einem wäß-rigen -wie bisher -, sondern in einem wasserfreien, organischen Lösungsmittel gelöst wird.In der vorliegenden Arbeit werden die Resultate über die Stabilität des NADH mitgeteilt, das in Ethylenglykol-Tris gelöst und während 136 Tagen bei den Temperaturen 2-8°C, 19-22°C, 35°C, 45°C und 60°C inkubiert wurde. Zum Vergleich wurde parallel dazu NADH in dest. Wasser gelöst und in gleicher Weise die Stabilität geprüft. Stabilization of reduced ß-nicotinamide-adenine-dinucleotide in an organic solventSummary: NADH is surprisingly stable, providing it is stored in anhydrous organic solvents, and not, as hitherto, in aqueous solvents. The stability of NADH was investigated in solution in ethylene glycol-Tris over a period of 136 days at temperatures of 2-8°C, 19-22°C, 35°C, 45°C and 60°C. For comparison, the stability of NADH in solution in distilled water was studied under similar conditions. Einleitung

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Non-enzymatic Interactions of Reduced Coenzyme I with Inorganic Phosphate and Certain Other Anions

Cited by 36 publications

References 7 publications

Mechanistic model for prediction of formate dehydrogenase kinetics under industrially relevant conditions

Mechanistic model for prediction of formate dehydrogenase kinetics under industrially relevant conditions

Mechanism of 3,4-dihydroxybenzaldehyde electropolymerization at carbon paste electrodes: catalytic detection of NADH

Stabilisierung des reduzierten β-Nicotinamid-Adenin-Dinucleotid in einem organischen Lösungsmittel

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