Effect of Niacin on Mitochondria of Allium Cepa Root Cells

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.

Role of the C-Terminal Tyrosine of Ferredoxin-Nicotinamide Adenine Dinucleotide Phosphate Reductase in the Electron Transfer Processes with Its Protein Partners Ferredoxin and Flavodoxin†

Biochemistry ◽

10.1021/bi049858h ◽

2004 ◽

Vol 43 (20) ◽

pp. 6127-6137 ◽

Cited By ~ 42

Author(s):

Isabel Nogués ◽

Jesús Tejero ◽

John K. Hurley ◽

Darío Paladini ◽

Susana Frago ◽

...

Keyword(s):

Electron Transfer ◽

Nicotinamide Adenine ◽

Transfer Processes ◽

Protein Partners ◽

Electron Transfer Processes

Incorporation of L-[1-14C]leucine into protein by liver postmitochondrial supernatant: opposing effects of preincubated nicotinamide-adenine dinucleotide phosphate and 4-dimethylamino-3′-methylazobenzene

Biochemical Journal ◽

10.1042/bj1460505 ◽

1975 ◽

Vol 146 (2) ◽

pp. 505-507 ◽

Cited By ~ 1

Author(s):

N P Madsen ◽

J E Labuc

Keyword(s):

Nicotinamide Adenine ◽

Free Protein ◽

A Cell ◽

Opposing Effects ◽

Stimulation Of

Combination of preincubated drug-metabolizing medium containing NADP+ with a cell-free protein-synthesizing system resulted in marked stimulation of incorporation of L-[1-14C]leucine into protein. Addition of 4-dimethylamino-3′-methylazobenzene, present and previously preincubated in the drug-metabolizing medium, decreased this effect.

20.BETA.-Hydroxysteroid dehydrogenase of neonatal pig testis: Cofactor requirement and stereospecificity of hydrogen transfer from nicotinamide adenine dinucleotide phosphate, reduced form.

Chemical and Pharmaceutical Bulletin ◽

10.1248/cpb.37.148 ◽

1989 ◽

Vol 37 (1) ◽

pp. 148-150 ◽

Cited By ~ 13

Author(s):

Shizuo NAKAJIN ◽

Shuji OHNO ◽

Masatada AOKI ◽

Masato SHINODA

Keyword(s):

Hydrogen Transfer ◽

Hydroxysteroid Dehydrogenase ◽

Nicotinamide Adenine ◽

Reduced Form ◽

Neonatal Pig

The stereochemistry of hydrogen transfer from reduced nicotinamide–adenine dinucleotide phosphate in the reduction of ethylenic linkages during cholesterol biosynthesis

Biochemical Journal ◽

10.1042/bj1190673 ◽

1970 ◽

Vol 119 (4) ◽

pp. 673-675 ◽

Cited By ~ 21

Author(s):

D. C. Wilton ◽

I. A. Watkinson ◽

M. Akhtar

Keyword(s):

Hydrogen Transfer ◽

Cholesterol Biosynthesis ◽

Reduced Nicotinamide Adenine Dinucleotide

Nicotinamide Adenine ◽

Double Bonds ◽

Hydride Ion ◽

It is shown that during the saturation of steroid carbon–carbon double bonds at Δ24,25 and Δ14,15 the `hydride ion' originates from the 4B side of the NADPH.

Microbial Oxidoreductases: Biotechnological and Synthetic Applications

International Journal of Research in Pharmaceutical Sciences ◽

10.26452/ijrps.v11i4.3535 ◽

2020 ◽

Vol 11 (4) ◽

pp. 6526-6531

Author(s):

Manas Ranjan ◽

Aashi Thakur ◽

Chirag Chopra ◽

Reena Singh

Keyword(s):

Industrial Applications ◽

Optically Active ◽

Nicotinamide Adenine ◽

Biological Oxidation ◽

Environmental Signals ◽

Synthetic Transformation ◽

A Cell ◽

Broad Specificity

Enzymes are biocatalysts responsible for driving all biochemical reactions in the cells. The enzymes determine the physiology of a cell and together regulate the growth and proliferation of cells in response to various environmental signals. The ability of cells to adapt and respond to environmental conditions can be utilized for industrial applications. Hydrolases and oxidoreductases are the most common classes of enzymes used in various industries such as pharmaceutical, food and beverages, bioremediation and biofuels, among others. Oxidoreductases are the EC1 class enzymes that catalyze the biological oxidation and reduction reactions. They transfer electrons from one molecule (reductant that donates electron) to other molecules (oxidants those accept electron). Usually, the enzymes of this class are NAD+ (Nicotinamide Adenine Dinucleotide) or NADP (Nicotinamide Adenine Dinucleotide Phosphate)-dependent. The oxidoreductases are a diverse class of enzymes responsible for catalyzing highly stereo selective and regioselective reactions, because of which they are the enzymes of choice for synthesis of optically-active compounds. Alcohol dehydrogenase (ADH) is one of the most studied oxidoreductases. Generally, ADHs have narrow specificity towards their substrates. Here we are looking for ADH having high/ broad specificity towards the substrate. This review discusses the enzyme oxidoreductase, synthetic transformation with oxidoreductase and application of oxidoreductase in bioremediation.