Flavin Adenine Dinucleotide - Catalysis

What is Flavin Adenine Dinucleotide (FAD)?

Flavin Adenine Dinucleotide (FAD) is a redox-active coenzyme associated with various enzymes, particularly those involved in oxidation-reduction reactions. It is derived from riboflavin (vitamin B2) and plays a critical role in cellular respiration.

How does FAD Function in Catalysis?

FAD functions as a versatile electron carrier in enzymatic reactions. It can exist in different redox states: FAD, FADH, and FADH2. During catalytic processes, FAD often cycles between oxidized (FAD) and reduced (FADH2) states, facilitating the transfer of electrons from one molecule to another.

What Enzymes Utilize FAD?

Several flavoenzymes utilize FAD as a cofactor. Notable examples include succinate dehydrogenase in the citric acid cycle and glucose oxidase in glucose metabolism. These enzymes play pivotal roles in energy production and metabolic pathways.

What is the Role of FAD in the Electron Transport Chain?

In the electron transport chain (ETC), FADH2 is crucial for ATP production. It donates electrons to Complex II (succinate dehydrogenase), which then transfers them to ubiquinone and subsequently through the ETC, ultimately leading to the formation of ATP through oxidative phosphorylation.

How is FAD Synthesized and Regenerated?

FAD is synthesized from riboflavin via a series of phosphorylation reactions. Enzymes like flavokinase and FAD synthetase are involved in this process. During catalytic cycles, FAD is regenerated through redox reactions, ensuring its continuous availability for enzymatic functions.

What are the Structural Features of FAD?

FAD consists of an adenine nucleotide linked to a flavin mononucleotide (FMN) via a phosphate group. This dual structure allows FAD to participate effectively in redox reactions, as the flavin moiety can accept and donate electrons.

Why is FAD Important in Catalysis?

FAD is essential in catalysis due to its ability to facilitate electron transfer reactions, which are fundamental to many biochemical processes. Its versatility and efficiency in converting between oxidized and reduced forms make it indispensable in metabolic and biosynthetic pathways.

Conclusion

Flavin Adenine Dinucleotide (FAD) is a critical coenzyme in the realm of catalysis. Its role in electron transfer, involvement in key metabolic enzymes, and participation in the electron transport chain underscore its importance in biochemical processes. Understanding FAD's mechanisms and functions provides insights into the intricate workings of cellular metabolism and energy production.

Relevant Publications

Assessing the impact of extracellular matrix fiber orientation on breast cancer cellular metabolism.

Issue Release: 2024

Metabolism of FAD, FMN and riboflavin (vitamin B2) in the human parasitic blood fluke Schistosoma mansoni.

Issue Release: 2024

Identification and Evaluation of Olive Phenolics in the Context of Amine Oxidase Enzyme Inhibition and Depression: In Silico Modelling and In Vitro Validation.

Issue Release: 2024

Structural insights into the bifunctional enzyme human FAD synthase.

Issue Release: 2024

Mining the Dynamical Properties of Substrate and FAD Binding Pockets of LSD1: Hints for New Inhibitor Design Direction.

Issue Release: 2024

Magnetic orientation in juvenile Atlantic herring () could involve cryptochrome 4 as a potential magnetoreceptor.

Issue Release: 2024

Understanding the Red Shift in the Absorption Spectrum of the FAD Cofactor in ClCry4 Protein.

Issue Release: 2024

Effects of deficiency or supplementation of riboflavin on energy metabolism: a systematic review with preclinical studies.

Issue Release: 2024

Inhibitory mechanism of Cr(VI) on sulfur-based denitrification: Bio-toxicity, bio-electron characteristics, and microbial evolution.

Issue Release: 2024

Multispectral Imaging of Metabolic Fluorophores: Comparing In Vivo and Fresh Ex Vivo Tissue.

Issue Release: 2024

Utilizing transcriptomics and metabolomics to unravel key genes and metabolites of maize seedlings in response to drought stress.

Issue Release: 2024

Structural insights into the semiquinone form of human Cytochrome P450 reductase by DEER distance measurements between a native flavin and a spin labelled non-canonical amino acid.

Issue Release: 2024

Enzymatic Galvanic Redox Potentiometry for In Vivo Biosensing.

Issue Release: 2024

Structure of human phagocyte NADPH oxidase in the activated state.

Issue Release: 2024

Metabolism of FAD, FMN and riboflavin (vitamin B2) in the human parasitic blood fluke .

Issue Release: 2024

Discovery of anticancer function of Febrifugine: Inhibition of cell proliferation, induction of apoptosis and suppression steroid synthesis in bladder cancer cells.

Issue Release: 2024

CHCHD4 binding affects the active site of apoptosis inducing factor (AIF): Structural determinants for allosteric regulation.

Issue Release: 2024

The in-silico study of the structural changes in the Arthrobacter globiformis choline oxidase induced by high temperature.

Issue Release: 2024

Cre-LoxP and tamoxifen-induced deletion of ovarian quiescin sulfhydryl oxidase 2 showed disruption of ovulatory activity in mice.

Issue Release: 2024

The dynamics of the flavin, NADPH, and active site loops determine the mechanism of activation of class B flavin-dependent monooxygenases.

Issue Release: 2024

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