Applications of Oxidoreductases

Diagnostic Tests ◽

Nicotinamide Adenine ◽

Organic Substrates ◽

Acceptor Molecule ◽

Practical Applications ◽

Oxidation Reduction ◽

Potential Applications

Oxidoreductases comprise of a large group of enzymes catalyzing the transfer of electrons from an electron donor to an electron acceptor molecule, commonly taking nicotinamide adenine dinucleotide phosphate (NADP) or nicotinamide adenine dinucleotide (NAD) as cofactors. Research on the potential applications of oxidoreductases on the growth of oxidoreductase-based diagnostic tests and better biosensors, in the design of inventive systems for crucial coenzymes regeneration, and in the creation of oxidoreductase-based approaches for synthesis of polymers and oxyfunctionalized organic substrates have made great progress. This chapter focuses on biocatalytic applications of oxidoreductases, since many chemical and biochemical transformations involve oxidation/reduction processes, developing practical applications of oxidoreductases has long been a significant target in biotechnology. Oxidoreductases are appropriate catalysts owing to their biodegradability, specificity and efficiency and may be employed as improved biocatalysts to substitute the toxic/expensive chemicals, save on energy/resources consumption, generate novel functionalities, or reduce complicated impacts on environment.

HYDROGENASE**Abbreviations: ATP, adenosine-5’-triphosphate; CoA, coenzyme A; DEAE-cellulose, diethylaminoethyl cellulose; E′o, oxidation-reduction potential at pH7; EPR, electron paramagnetic resonance; FAD, flavin adenine dinucleotide; FMN, flavin mononucleotide; Fd, ferredoxin; MB, methylene blue; MV, methyl viologen; NAD+ and NADH, nicotinamide adenine dinucleotide and its reduced form; NADP+ and NADPH, nicotinamide adenine dinucleotide phosphate and its reduced form; TPP, thiamine pyrophosphate.

Microbial Iron Metabolism ◽

10.1016/b978-0-12-515250-1.50016-3 ◽

1974 ◽

pp. 231-282 ◽

Cited By ~ 33

Author(s):

LEONARD E. MORTENSON ◽

JIANN-SHIN CHEN

Keyword(s):

Deae Cellulose ◽

Thiamine Pyrophosphate ◽

Nicotinamide Adenine ◽

Reduced Form ◽

Flavin Mononucleotide ◽

Paramagnetic Resonance ◽

Oxidation Reduction ◽

Oxidation Reduction Potential

Oxidoreductases: Significance for Humans and Microorganism

10.5772/intechopen.93961 ◽

2020 ◽

Author(s):

Hussein Mahdi Kareem

Keyword(s):

Large Class ◽

Electron Donor ◽

Electron Acceptor ◽

Diagnostic Tests ◽

Organic Substrates ◽

Biochemical Reactions ◽

Biomass Processing ◽

Oxidation Reduction ◽

Special Case ◽

Made In

Oxidoreductases consist of a large class of enzymes catalyzing the transfer of electrons from an electron donor (reductant) to an electron acceptor (oxidant) molecule. Since so many chemical and biochemical transformations comprise oxidation/reduction processes, it has long been an important goal in biotechnology to develop practical biocatalytic applications of oxidoreductases. During the past few years, significant breakthrough has been made in the development of oxidoreductase-based diagnostic tests and improved biosensors, and the design of innovative systems for the regeneration of essential coenzymes. Research on the construction of bioreactors for pollutants biodegradation and biomass processing, and the development of oxidoreductase-based approaches for synthesis of polymers and functionalized organic substrates have made great progress. Proper names of oxidoreductases are in a form of “donor:acceptor oxidoreductase”; while in most cases “donor dehydrogenase” is much more common. Common names also sometimes appeared as “acceptor reductase”, such as NAD+ reductase. “Donor oxidase” is a special case when O2 serves as the acceptor. In biochemical reactions, the redox reactions are sometimes more difficult to observe, such as this reaction from glycolysis: Pi + glyceraldehyde-3-phosphate + NAD+ → NADH + H+ + 1,3-bisphosphoglycerate, where NAD+ is the oxidant (electron acceptor), and glyceraldehyde-3-phosphate functions as reductant (electron donor).

Oxidation−Reduction Properties of the Regulatory Disulfides of Sorghum Chloroplast Nicotinamide Adenine Dinucleotide Phosphate−Malate Dehydrogenase†

Biochemistry ◽

10.1021/bi9916731 ◽

2000 ◽

Vol 39 (12) ◽

pp. 3344-3350 ◽

Cited By ~ 38

Author(s):

Masakazu Hirasawa ◽

Eric Ruelland ◽

Isabelle Schepens ◽

Emmanuelle Issakidis-Bourguet ◽

Myroslawa Miginiac-Maslow ◽

...

Keyword(s):

Malate Dehydrogenase ◽

Nicotinamide Adenine ◽

Oxidation Reduction

Changes in phosphorylation of adenosine phosphate and redox state of nicotinamide-adenine dinucleotide (phosphate) in Geobacter sulfurreducens in response to electron acceptor and anode potential variation

Bioelectrochemistry ◽

10.1016/j.bioelechem.2015.03.003 ◽

2015 ◽

Vol 106 ◽

pp. 213-220 ◽

Cited By ~ 9

Author(s):

Nicholas D. Rose ◽

John M. Regan

Keyword(s):

Electron Acceptor ◽

Redox State ◽

Geobacter Sulfurreducens ◽

Nicotinamide Adenine ◽

Anode Potential ◽

Potential Variation ◽

Adenosine Phosphate

Effect of Niacin on Mitochondria of Allium Cepa Root Cells

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100060404 ◽

1967 ◽

Vol 25 ◽

pp. 78-79

Author(s):

M. Arif Hayat

Keyword(s):

Hydrogen Transfer ◽

Nicotinamide Adenine ◽

Root Tips ◽

Root Cells ◽

Transfer Processes ◽

Standard Procedures ◽

A Cell ◽

Critical Interest

Although it is recognized that niacin (pyridine-3-carboxylic acid), incorporated as the amide in nicotinamide adenine dinucleotide (NAD) or in nicotinamide adenine dinucleotide phosphate (NADP), is a cofactor in hydrogen transfer in numerous enzyme reactions in all organisms studied, virtually no information is available on the effect of this vitamin on a cell at the submicroscopic level. Since mitochondria act as sites for many hydrogen transfer processes, the possible response of mitochondria to niacin treatment is, therefore, of critical interest.Onion bulbs were placed on vials filled with double distilled water in the dark at 25°C. After two days the bulbs and newly developed root system were transferred to vials containing 0.1% niacin. Root tips were collected at ¼, ½, 1, 2, 4, and 8 hr. intervals after treatment. The tissues were fixed in glutaraldehyde-OsO4 as well as in 2% KMnO4 according to standard procedures. In both cases, the tissues were dehydrated in an acetone series and embedded in Reynolds' lead citrate for 3-10 minutes.