Biochemistry Terms Starting With F
Biochemistry Glossary: F
Fatty Acid
/ FAT-ee AS-id / · Latin adipem (fat) + acidus (sour)
Fatty acid is a carboxylic acid with a long hydrocarbon chain that forms a fundamental structural and energetic component of lipids.
Fatty acids range from 4 to 36 carbon atoms in length, with palmitic acid (16 carbons) and stearic acid (18 carbons) among the most abundant in human tissue. Saturated fatty acids carry only single bonds between carbons and pack tightly into solid structures at room temperature, while unsaturated fatty acids contain one or more double bonds that introduce kinks, keeping them liquid. Complete oxidation of one molecule of palmitic acid through beta-oxidation and the citric acid cycle yields approximately 129 ATP molecules.
Omega-3 and omega-6 fatty acids cannot be synthesized by humans because the enzymes needed to insert double bonds beyond carbon 9 are absent, making dietary sources from fish, flaxseed, and walnuts necessary.
Greenland sharks (Somniosus microcephalus) accumulate trimethylamine oxide and unusual polyunsaturated fatty acids in their tissues as cryoprotectants, allowing them to remain active in seawater as cold as -2°C.
Building Blocks of Lipids →All fats are unhealthy. Omega-3 fatty acids such as EPA and DHA are structural components of cell membranes and precursors to anti-inflammatory signaling molecules that the body cannot produce without a dietary supply.
Atlantic salmon (Salmo salar) synthesize EPA and DHA from shorter-chain omega-3 precursors and deposit these fatty acids in muscle tissue at concentrations of roughly 1 to 2 grams per 100 grams of fillet, one of the highest levels found in any commonly consumed food.
Feedback Inhibition
/ FEED-back in-hi-BISH-un / · English feedback (information returned) + Latin inhibere (to restrain)
Feedback inhibition is a regulatory mechanism in which the end product of a metabolic pathway binds to and inhibits the first committed enzyme in that pathway, reducing further production of that product.
This mechanism prevents overproduction of metabolites and conserves the raw materials and energy a cell would otherwise waste. In Escherichia coli, the amino acid threonine inhibits aspartokinase, the enzyme catalyzing the first step in threonine biosynthesis, when intracellular threonine concentrations reach approximately 1 mM. Inhibition occurs through allosteric binding, meaning threonine attaches to a regulatory site distinct from the enzyme’s active site and changes the enzyme’s shape to reduce its activity.
Because inhibition targets the first committed step rather than a later one, no unnecessary intermediates accumulate in the pathway.
Isoleucine biosynthesis in E. coli was one of the first metabolic pathways in which feedback inhibition was experimentally demonstrated, by Edwin Umbarger in 1956, establishing the concept that end products could regulate their own synthesis.
Feedback inhibition shuts down the last enzyme in a metabolic pathway. It targets the first committed step, so intermediates do not build up and cellular resources are conserved before any unnecessary products form.
In yeast (Saccharomyces cerevisiae), excess histidine binds to the first enzyme in the histidine biosynthesis pathway, ATP phosphoribosyltransferase, reducing its activity and halting production within minutes of histidine reaching sufficient intracellular levels.
Fermentation
/fer-men-TAY-shun/ · Latin fermentum (leaven, yeast)
Fermentation is an anaerobic metabolic process in which cells regenerate NAD+ by transferring electrons from NADH to organic molecules, sustaining glycolysis without oxygen.
During alcoholic fermentation, Saccharomyces cerevisiae converts pyruvate to ethanol and carbon dioxide, regenerating the NAD+ that glycolysis requires to continue oxidizing glucose. Lactic acid bacteria such as Lactobacillus acidophilus reduce pyruvate directly to lactate, a reaction that also regenerates NAD+ and lowers the pH of the surrounding environment. Both pathways yield only 2 ATP per glucose molecule, compared with the 36 to 38 ATP generated by aerobic respiration.
Human skeletal muscle cells temporarily use lactic acid fermentation during intense exercise when oxygen delivery cannot keep pace with energy demand, allowing glycolysis to continue for short bursts of high-power output.
Fermentation chemistry was first described mechanistically by Eduard Buchner in 1897, when he demonstrated that cell-free yeast extracts could ferment sugar to ethanol, overturning the prevailing belief that living cells were required and earning him the 1907 Nobel Prize in Chemistry.
Fermentation Biology →Fermentation produces only alcohol. Different organisms use fermentation to generate lactic acid in yogurt, acetic acid in vinegar, and butyric acid in certain cheeses, depending on which organic molecule accepts the electrons from NADH.
Escherichia coli switches to mixed-acid fermentation when oxygen is absent in the human large intestine, producing formate, acetate, ethanol, and hydrogen gas in ratios that shift with gut pH and substrate availability.
Flavin Adenine Dinucleotide
/ FLAY-vin AD-e-neen dy-NU-klee-o-tide / · Latin flavus (yellow) + Arabic al-danin (adenine) + Greek dis (two) + Latin nucleus (kernel)
Flavin adenine dinucleotide is a redox cofactor derived from riboflavin that carries electrons between metabolic reactions by cycling between its oxidized form, FAD, and its reduced form, FADH2.
FAD consists of a flavin mononucleotide unit linked to adenosine monophosphate through a phosphoanhydride bond, giving the molecule its characteristic yellow color in solution. During the citric acid cycle, the enzyme succinate dehydrogenase uses FAD as a tightly bound prosthetic group to oxidize succinate to fumarate, accepting two electrons and two protons to become FADH2. FADH2 then donates its electrons directly to Complex II of the mitochondrial electron transport chain, ultimately contributing to the synthesis of approximately 1.5 ATP molecules per FADH2 oxidized, fewer than the 2.5 ATP generated per NADH.
The lower reduction potential of FAD relative to NAD+ makes it better suited for oxidizing substrates that are already partially oxidized, such as succinate.
Riboflavin deficiency (vitamin B2 deficiency) impairs FAD synthesis and causes ariboflavinosis, a condition characterized by cracked lips, inflamed tongue, and sensitivity to light, documented in populations whose diets lack dairy, meat, and leafy greens.
FAD and FADH2 are interchangeable names for the same molecule. FAD is the oxidized electron acceptor and FADH2 is the reduced electron carrier; they differ in both chemical structure and reduction potential, and only FADH2 can donate electrons to the transport chain.
The enzyme acyl-CoA dehydrogenase in human liver mitochondria uses FAD to remove two hydrogen atoms from fatty acyl-CoA during the first step of beta-oxidation, generating FADH2 and introducing a double bond into the fatty acid chain.
Flavin Mononucleotide
/FLAY-vin mon-oh-NEW-klee-oh-tide/ · Latin flavus (yellow) + Greek monos (single) + Latin nucleus (kernel) + Greek -otes (condition)
Flavin mononucleotide is a riboflavin-derived coenzyme that carries electrons in oxidation-reduction reactions and binds as a prosthetic group to the first complex of the mitochondrial electron transport chain.
FMN consists of riboflavin with a phosphate group attached at the 5′ position of its ribitol chain, making it structurally simpler than FAD, which carries an additional adenosine monophosphate unit. Within Complex I of the mitochondrial electron transport chain, FMN accepts two electrons from NADH and passes them sequentially to a series of iron-sulfur clusters, with a standard reduction potential of approximately -0.22 volts. Unlike many coenzymes that associate loosely with enzymes, FMN binds tightly as a prosthetic group and does not dissociate between catalytic cycles.
FMN can also exist in a one-electron-reduced semiquinone radical state, an intermediate that allows it to bridge reactions between two-electron donors and one-electron acceptors.
Riboflavin, the dietary precursor to FMN, was first isolated in 1933 by Richard Kuhn and colleagues from whey, and its structure was confirmed by synthesis in 1935, establishing the chemical basis for understanding flavin electron carriers.
FMN and FAD are identical molecules. FMN lacks the adenosine monophosphate portion present in FAD, making it a structurally distinct and smaller cofactor with a different binding affinity for its target enzymes.
The enzyme NADH dehydrogenase in Escherichia coli uses FMN as its primary electron acceptor, transferring electrons from NADH to membrane-bound quinones at a rate sufficient to sustain the proton gradient needed for ATP synthesis under aerobic conditions.
Free Energy
/FREE EN-er-jee/ · Greek eleutheros (free) + energeia (activity, operation)
Free energy is the thermodynamic quantity that measures the maximum useful work a system can perform at constant temperature and pressure, represented by the Gibbs free energy function.
Biochemists express free energy changes as delta G, where a negative value indicates a spontaneous reaction that releases energy and a positive value indicates a reaction that requires an energy input to proceed. ATP hydrolysis releases approximately 30.5 kJ/mol of free energy under standard conditions, but this value rises to about 50 kJ/mol inside living cells because of the low concentrations of ADP and phosphate maintained there. E.
coli and other organisms couple exergonic reactions to endergonic ones so that the combined delta G remains negative, driving biosynthetic reactions that would otherwise stall. Temperature and concentration both shift the actual free energy change away from the standard value, which is why cellular conditions matter as much as the reaction chemistry itself.
Josiah Willard Gibbs developed the mathematical framework for free energy in the 1870s without ever studying a biological system, yet his equations now underpin every quantitative description of metabolic spontaneity and enzyme-driven reaction coupling in modern biochemistry.
Free energy means energy that is available at no cost. Free energy describes the portion of a system's total energy that can do work under specific conditions of temperature and pressure, and every spontaneous reaction consumes some of it.
During bioluminescence in the deep-sea lanternfish (Myctophum punctatum), the oxidation of luciferin releases free energy with a delta G negative enough to excite a product molecule to an electronic state that emits light near 480 nm, converting chemical free energy directly into photons.
Fructose
/FRUK-tohz/ · Latin fructus (fruit)
Fructose is a six-carbon ketose monosaccharide found naturally in fruits, honey, and root vegetables, and is the sweetest of the common dietary sugars.
Fructose shares the molecular formula C6H12O6 with glucose but differs in structure: its carbonyl group sits at carbon 2, making it a ketose, while glucose carries its carbonyl at carbon 1 as an aldose. At roughly 1.7 times the sweetness of sucrose, fructose requires smaller quantities to achieve the same perceived sweetness in food products. Unlike glucose, which is metabolized in nearly every cell, fructose is processed almost exclusively in the liver, where it enters glycolysis below the main regulatory checkpoint controlled by phosphofructokinase-1.
High fructose intake can therefore drive hepatic lipogenesis at rates that bypass normal feedback controls, contributing to elevated triglycerides and non-alcoholic fatty liver disease in clinical studies.
High-fructose corn syrup was developed in Japan in the 1960s and introduced into the US food supply in the 1970s; by 2000, Americans consumed an average of about 63 grams of added fructose per day, more than double the estimated intake from the early 20th century.
Fructose from fruit is harmless while fructose from processed foods is harmful. The liver processes fructose through the same biochemical pathway regardless of its source, and excessive intake from any source can elevate liver fat and blood triglycerides.
Honeybees (Apis mellifera) hydrolyze sucrose from flower nectar using the enzyme invertase, depositing the resulting fructose and glucose into honeycomb cells where water evaporates to produce honey containing roughly 38 to 40% fructose by weight.
Functional Group
/FUNK-shun-al groop/ · Latin functio (performance) + Greek -al (relating to) + Old English grupe (cluster)
Functional group is a specific arrangement of atoms within a molecule that determines the chemical properties and reactivity of that compound.
Each functional group confers predictable chemical behavior on any molecule that contains it. The hydroxyl group (-OH) in glucose makes this sugar highly soluble in water, while the carboxyl group (-COOH) in fatty acids gives them their acidic properties and allows them to form ester bonds with glycerol. Many biomolecules carry more than one functional group simultaneously; amino acids, for example, contain both an amino group (-NH2) and a carboxyl group (-COOH), which together allow them to act as buffers and to form peptide bonds during protein synthesis.
The thiol group (-SH) found in the amino acid cysteine can form disulfide bridges between protein chains, and these cross-links are what give human hair its mechanical strength and allow it to hold a curl.
Building Blocks of Proteins →Functional groups only affect whether a molecule dissolves in water. They strongly shape how the whole molecule reacts with enzymes, responds to pH changes, and interacts with other molecules in cells.
The phosphate group in adenosine triphosphate carries a large negative charge at physiological pH, which traps the molecule inside the cell membrane and concentrates chemical energy in a form that kinases can transfer directly to substrate proteins.
