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Journal of Plant Biochemistry & Physiology

Journal of Plant Biochemistry & Physiology
Open Access

ISSN: 2329-9029

Commentary - (2023)Volume 11, Issue 3

Unveiling the Vital Role of FADH2 in Metabolism

Zovinh Aliot*
 
*Correspondence: Zovinh Aliot, Department of Medical Physiology, Mekelle University, Mekelle, Ethiopia, Email:

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Description

In the intricate world of plant biology, the process of energy conversion is important for biochemical reactions. The Electron Transport Chain (ETC), a vital process responsible for generating Adenosine Triphosphate (ATP), the energy currency of cells. While much has been said about the role of Nicotinamide Adenine Dinucleotide (NADH), Flavin Adenine Dinucleotide (FADH2) has a vital role in this process. Electron transport chain is a remarkable process occurs within the inner mitochondrial membrane of plant cells (just as it does in animal cells) and is important for the production of ATP, the primary energy currency used by cells. The ETC is a series of protein complexes and electron carriers that shuttle high-energy electrons derived from the breakdown of glucose and other organic molecules through a sequence of redox reactions. These electrons gradually lose their energy as they move through the chain and, in doing so, pump protons (H+) across the inner mitochondrial membrane into the intermembrane space, creating a proton gradient. This gradient, also known as the proton motive force, drives the production of ATP.

The key components of the electron transport chain include NADH, FADH2, a series of protein complexes (I, II, III, and IV), and two mobile electron carriers, ubiquinone (Coenzyme Q) and cytochrome c. While NADH is usually in the spotlight due to its role in complex I, FADH2 plays a pivotal role in complex II and complements the overall functioning of the ETC.

Role of FAD

Flavin Adenine Dinucleotide (FAD) is a coenzyme that plays a central role in various metabolic processes, including the ETC. FAD is derived from riboflavin, also known as vitamin B2, which is an essential nutrient for plants and animals alike. When FAD accepts two hydrogen atoms and two electrons, it becomes reduced and transforms into FADH2. This FADH2 is important in complex II of the electron transport chain. Complex II, also known as Succinate Dehydrogenase (SDH), is the entry point for FADH2 into the electron transport chain. This complex holds a unique position in the ETC as it connects the TCA (Tricarboxylic Acid) cycle, also known as the citric acid cycle or Krebs cycle, with the ETC.

Mechanism of metabolism

TCA cycle connection: In the TCA cycle, organic molecules, such as succinate, undergo a series of reactions that ultimately produce FADH2. Succinate, in particular, is oxidized by succinate dehydrogenase, leading to the formation of FADH2.

FADH2 formation: This FADH2 produced in the TCA cycle is directly transferred to complex II. Here, succinate dehydrogenase catalyzes the conversion of succinate to fumarate while simultaneously transferring electrons from FADH2 to FAD, converting it back into its oxidized form, FAD. The electrons derived from FADH2 are then transferred to the electron transport chain.

Electron transfer: Once the electrons are transferred to the ETC, they enter the chain at the level of ubiquinone (Coenzyme Q), specifically in complex III. From here, they proceed through the chain, ultimately driving the pumping of protons and ATP synthesis.

Role of FADH2

FADH2, despite being somewhat overshadowed by NADH, plays a crucial role in the overall efficiency of the electron transport chain and ATP production. Here are a few reasons for FADH2 importance in metabolism:

ATP production: FADH2 contributes to ATP production in the electron transport chain. While NADH transfers electrons early in the chain at complex I, FADH2 enters later at complex II. This means that electrons derived from FADH2 skip the initial proton-pumping step, contributing to a slightly lower proton motive force. As a result, the electrons from FADH2 generate fewer ATP molecules than those from NADH. However, they still play a significant role in overall energy production.

Redox balance: The presence of FADH2 in complex II helps maintain redox balance in the cell. The TCA cycle, in which FADH2 is generated, is essential for the breakdown of various organic molecules, not just glucose. By participating in this cycle, FADH2 ensures that the ETC can receive electrons from a variety of metabolic pathways, helping to maintain the cell's energy balance.

Metabolic flexibility: Plants, like all organisms, must adapt to varying environmental conditions and energy demands. The presence of FADH2 in complex II provides metabolic flexibility. Depending on the metabolic pathways being utilized, FADH2 can be generated and directed into the electron transport chain, contributing to ATP production when needed.

Conclusion

In the world of plant biology, the Electron Transport Chain unfolds as a mesmerizing performance, with FADH2 playing a crucial but often overlooked role. This is derived from the TCA cycle, enters the chain at complex II, contributing to ATP production and helping maintain redox balance in the cell. While NADH may take center stage in discussions about the ETC, it is important to recognize that FADH2 is a vital player, allowing plants to adapt to changing energy demands and maintain metabolic flexibility. As we continue to unravel the intricate processes within plant cells, our appreciation for the role of FADH2 in sustaining life on Earth deepens, reminding us of the remarkable complexity and resilience of the natural world.

Author Info

Zovinh Aliot*
 
Department of Medical Physiology, Mekelle University, Mekelle, Ethiopia
 

Citation: Aliot Z (2023) Unveiling the Vital Role of FADH2 in Metabolism. J Plant Biochem Physiol. S 11:276

Received: 25-Jul-2023, Manuscript No. JPBP-23-27190; Editor assigned: 27-Jul-2023, Pre QC No. JPBP-23-27190; Reviewed: 10-Aug-2023, QC No. JPBP-23-27190; Revised: 17-Aug-2023, Manuscript No. JPBP-23-27190; Published: 24-Aug-2023 , DOI: 10.35248/2329-9029.23.11.276

Copyright: © 2023 Aliot Z. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original author and source are credited

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