Biomimetic cofactors and methods for their recycling

Zachos, Ioannis; Nowak, Claudia; Sieber, Volker

doi:10.1016/j.cbpa.2018.10.003

Cited by 59 publications

(74 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…NCBs are used in redox biocatalysis as alternatives to NAD(P)(H) and were recently reviewed . In this study, we investigated the applicability of NCBs (Figure ) for the enzymatic regioselective hydroxylation of aromatic compounds with several flavoenzymes (Figure ).…”

Section: Discussionmentioning

confidence: 99%

Flavoenzyme‐mediated Regioselective Aromatic Hydroxylation with Coenzyme Biomimetics

et al. 2020

View full text Add to dashboard Cite

Regioselective aromatic hydroxylation is desirable for the production of valuable compounds. External flavin‐containing monooxygenases activate and selectively incorporate an oxygen atom in phenolic compounds through flavin reduction by the nicotinamide adenine dinucleotide coenzyme, and subsequent reaction with molecular oxygen. This study provides the proof of principle of flavoenzyme‐catalyzed selective aromatic hydroxylation with coenzyme biomimetics. The carbamoylmethyl‐substituted biomimetic in particular affords full conversion in less than two hours for the selective hydroxylation of 5 mM 3‐ and 4‐hydroxybenzoates, displaying similar rates as with NADH, achieving a 10 mM/h enzymatic conversion of the medicinal product gentisate. This biomimetic appears to generate less uncoupling of hydroxylation that typically leads to undesired hydrogen peroxide. Therefore, we show these flavoenzymes have the potential to be applied in combination with biomimetics.

show abstract

Section: Discussionmentioning

confidence: 99%

Flavoenzyme‐mediated Regioselective Aromatic Hydroxylation with Coenzyme Biomimetics

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Nevertheless, significant efforts are undertaken to develop simpler, more efficient alternatives [5,8]. Natural-based NADH analogues have been used to investigate the influence of substituents on the dihydropyridine ring, and synthetic nicotinamide coenzyme biomimetics (NCBs) were produced to investigate the hydride transfer mechanism, but more recently were attractive to provide inexpensive alternative coenzymes ( Figure 1) [5,[9][10][11].…”

Section: Alternative Coenzymes For Oxidoreductasesmentioning

confidence: 99%

“…To date, the regeneration of NCBs has been limited to chemical, chemoenzymatic and electrochemical methods, because of the lack of dehydrogenases able to accept those biomimetics [5,11,24]. Recently, a glucose dehydrogenase from Sulfolobus sulfataricus (SsGDH) and its variants were tested with BNA, P2NA and P3NA (Figures 3 and 4b).…”

Section: Coenzymes For Nad(p)-dependent Dehydrogenases Enzymatic Ncbmentioning

confidence: 99%

Alternative coenzymes for biocatalysis

Guarneri

Berkel

Paul

2019

Current Opinion in Biotechnology

View full text Add to dashboard Cite

Coenzymes are ubiquitous in Nature, assisting in enzymecatalysed reactions. Several coenzymes, nicotinamides and flavins, have been known for close to a century, whereas variations of those organic molecules have more recently come to light. In general, the requirement of these coenzymes imposes certain constraints for in vitro enzyme use in biocatalytic processes. Alternative coenzymes have risen to circumvent the cost factor, tune reaction rates or obtain different chemical reactivity. This review will focus on these alternatives and their role and applications in biocatalysis.

show abstract

“…The rare fully biocatalytic strategies rely on the coupled-enzyme approach with engineered glucose dehydrogenase. 31,32 In this review, we shall concentrate on enzymatic redox reactions which utilize NAD(P) as a hydride shuttle, not excluding those enzymes which rely on an additional mediator (flavin, heme-bound iron, iron-sulfur cluster). Importantly, NAD(P) is usually bound non-covalently and can diffuse in and out of the enzymes, depending on the enzyme affinity for the cofactor.…”

Section: Introductionmentioning

confidence: 99%