Enzymic coupling with

The flavin reductase has been purified by several researchers. This enzyme from R. erythropolis IGTS8 was partially purified by Ohshiro et al., and reported to have an optimum pH and temperature of 6.0 and 35°C, respectively [153], The DszD enzyme from IGTS8 was also purified [53] and reported to be of 25 kDa size however, no kinetic details related to DszD were reported. This enzyme couples with FMN with NADH to produce reduced flavin required for DszC and DszA catalyzed reactions. 

Another type of sensor was based on the utilization of glucose dehydrogenase enzyme coupling with /ra(2,2 -bipyridylruthenium(II) complex [31]. This sensor can be used in the 10-2500-pmol/L concentration range. Several interferences occur, like NADH, oxalate, proline, and tripropylamine. However, gluconic acid and NAD+ do not interfere. 

M. J. Kim, Y. Ahn, and J. Park, Dynamic kinetic resolutions and asymmetric transformations by enzymes couples with metal catalysis, Curr. Opin. Biotechnol. 2002, 13, 578-587. 

Dynamic Kinetic Resolutions by Enzymes Coupled with Metal Catalysts... 

FIGURE 17.11 Enzyme-catalyzed reduction of pyruvate to (S)-(+)-lactate. A preferred orientation of binding of pyruvate to the enzyme, coupled with a prescribed location of the reducing agent, the coenzyme NADH, leads to hydrogen transfer exclusively to a single face of the carbonyl group. 

Kim Y-S, Kara M, Ikebukuro K, Miyake J, Ohkawa H, Karube 1 (1996) Photo-induced activation of cytochrome P450/reductase fusion enzyme coupled with spinach chloroplasts. Biotechnol Tech 10 717-720... 

Most of us anticipated that ribosyl activation for nucleotide biosynthesis would use the same device of phosphorylation, so well known for glucose. But the novelty of pyrophos-phorylation used by this enzyme (coupled with elimination of inorganic pyrophosphate upon subsequent condensations) established my unalloyed awe for the ingenuity and fitness of an enzyme. 

In 2011, alcohol dehydrogenase (ADH) was used as a model enzyme coupled with poly (MG) for NADH reoxidation in the construction of a three-dimensional BFC with ethanol as fuel [103]. In combination with an air-breathing/gas difhision cathode (using laccase as an oxygen reduction enzyme), a BFC was fabricated that was able to successfully exploit ethanol oxidation by an NAD -dependent ADH, immobilized by entrapment in a multiwaUed CNT (MWCNT)/chitosan matrix [106]. The feasibility and reproducibUity of the resulting BFC were demonstrated in 2008 with a series of standardized multilaboratory experiments [96]. 

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