FAD full form in biology

By: Prof. Dr. Fazal Rehman | Last updated: February 3, 2024

FAD full form in biology
  • In biology, the term “FAD” stands for “Flavin Adenine Dinucleotide.
  • It is derived from riboflavin (vitamin B2) and is an essential component of several enzymes.
Functions                       Description
Role as an electron carrier ·        FAD serves as an electron carrier in the process of cellular respiration and ·        It transfers the electrons to the electron transport chain.
Role in feedback Regulation of Krebs cycle ·        FAD is involved in feedback regulation by influencing the rate of cycle based on the energy requirements of the cell.
Role in Citric acid cycle ·        It is a cofactor in enzymes like succinate dehydrogenase, which participates in the citric acid cycle (Krebs cycle) ·        Helps in the production of ATP and CO2.
Role in the oxidation of Fatty Acids ·        FAD assists in the breakdown of fatty acids into acetyl-CoA, which can be used for energy production.
 

Different forms of FAD:

Forms        FAD   FADH FADH2
  State         ·       Oxidized     ·       Partially reduced   ·       Reduced
Structure     ·       Dinucleotide coenzyme with two adenine bases, a ribose sugar, and a flavin mononucleotide (FMN) unit ·       One unpaired electron on the flavin mononucleotide (FMNH) unit. ·       Dinucleotide coenzyme with one additional hydrogen atom on the flavin mononucleotide (FMNH) unit.
  Function     ·       Acts as an electron acceptor ·       Can participate in electron transfer reactions. ·       An unstable radical species. ·       Acts as an electron donor to form FAD. ·       Serves as a temporary electron carrier in cellular respiration.
 

Comparison between FAD and NAD

Aspect                FAD               NAD
Full form ·        Flavin Adenine Dinucleotide ·        Nicotinamide Adenine Dinucleotide
Discoverer ·        Hugo Theorell ·        Sir Arthur Harden and William John Young
Year of discovery ·        1937 (Structure) ·        1949 (As a coenzyme) ·        1906-1907
Derived from ·        Riboflavin vitamin B2 ·        Nicotinamide vitamin B3
Coenzyme Type ·        Flavoprotein – contains flavin as a prosthetic group. ·        Dinucleotide coenzyme – contains nicotinamid as a prosthetic group.
Structural formula    
Molar mass ·        785.5497 g/mol ·        663.43 g/mol
Forms ·        FAD (oxidized form) ·        FADH2 (reduced form) ·        NAD+ (oxidized form) ·        NADH (reduced form)
Color ·        Yellow (oxidized) ·        Colorless (reduced) ·        Colorless (NAD+) ·        Light blue (NADH)
Redox Reactions ·        Accepts 2 electrons and 2 protons in reduction. ·        Donates 2 electrons and 2 protons in oxidation. ·        Accepts 2 electrons and 1 proton in reduction. ·        Donates 2 electrons and 1 proton in oxidation.
Cellular Processes ·        Involved in the citric acid cycle (Krebs cycle) ·        fatty acid oxidation ·        Electron transport chain ·        Participates in glycolysis ·        the citric acid Cycle ·        electron transport chain during cellular respiration ·        Other metabolic pathways
 

Comparison between FAD and FADH:

Aspect       FAD                    FADH
Role in Electron Transfer ·        Accepts two electrons and two protons in reduction reactions to become FADH2 ·        Donates two electrons and two protons in oxidation reactions to become FAD
Color ·        Yellow in its oxidized form ·        Colorless or pale yellow in its reduced form
Energy Level ·        Energy in the molecule is lower ·        Energy in the molecule is high
Function ·        Acts as an electron carrier, accepting and donating electrons in redox reactions ·        Functions as a temporary electron carrier, donating electrons to the electron transport chain for ATP synthesis
Type of coenzyme ·        Flavoprotein – contains flavin as a prosthetic group ·        Flavoprotein – contains flavin as a prosthetic group
Stability ·        Stable ·        Less stable
Involvement in Cellular Processes     ·        Participates in the citric acid cycle (Krebs cycle) ·        Fatty acid oxidation ·        Electron transfer reactions in the mitochondrial respiratory chain ·        Involved in the electron transport chain during cellular respiration ·        Contributing to oxidative phosphorylation and ATP production  
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