Energy, Chemical Reactions, and Enzymes in Organisms

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86 Terms

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Energy

Required for all cellular activities and functions.

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Producers

Organisms that convert CO2 and water into sugars.

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Photosynthesis

Process converting sunlight into chemical energy.

<p>Process converting sunlight into chemical energy.</p>
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Consumers

Organisms that obtain energy by eating producers.

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Metabolism

Total of all chemical reactions in cells.

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Anabolic reactions

Build larger molecules from smaller ones.

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Catabolic reactions

Break down large molecules into smaller ones.

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Potential Energy

Stored energy with the potential to do work.

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Kinetic Energy

Energy associated with movement and activity.

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Chemical Bond Energy

Energy stored in chemical bonds of molecules.

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First Law of Thermodynamics

Energy cannot be created or destroyed, only transformed.

<p>Energy cannot be created or destroyed, only transformed.</p>
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Entropy

Measure of disorder in a system.

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Second Law of Thermodynamics

Energy conversions are never 100% efficient.

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Heat

Energy transfer that increases molecular motion.

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Mechanical Energy

Energy used in muscle movement.

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Energy Efficiency

Percentage of energy converted to useful work.

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Cellular Respiration

Process of breaking down glucose for energy.

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ATP

Energy currency of the cell.

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Vesicles

Small membrane-bound sacs transporting materials.

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Motor Proteins

Proteins that move vesicles within cells.

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Immune Cells

Cells that patrol the body for pathogens.

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Nerve Cells

Cells that transmit signals throughout the body.

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Heart Cells

Cells that contract to pump blood.

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Concentration Gradient

Difference in concentration across a membrane.

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Electric Charge Imbalance

Difference in charge distribution across a membrane.

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Ecological Pyramid

Representation of energy flow in ecosystems.

<p>Representation of energy flow in ecosystems.</p>
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Energy Replenishment

Constant need for energy supply in organisms.

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Gibb's Free Energy (G)

Usable energy for cellular reactions.

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Entropy (S)

Unusable energy lost to disorder.

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Enthalpy (H)

Total energy in a system.

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ΔG

Change in usable energy for a reaction.

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Endergonic Reactions

Require energy input, ΔG is positive.

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Exergonic Reactions

Release energy, ΔG is negative.

<p>Release energy, ΔG is negative.</p>
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Anabolic Reactions

Building processes, typically endergonic.

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Catabolic Reactions

Breaking processes, typically exergonic.

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ATP

Main energy currency of the cell.

<p>Main energy currency of the cell.</p>
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ADP

Adenosine diphosphate, precursor to ATP.

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Activation Energy (Ea)

Energy needed to initiate a reaction.

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Transition State

Unstable state during a reaction.

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Enzymes

Proteins that speed up biochemical reactions.

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Enzyme-Substrate Complex

Temporary complex formed during enzyme action.

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Active Site

Region where substrate binds on an enzyme.

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Kinetic Energy

Energy of motion, needed for reactions.

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Hydrolysis Reaction

Breaking bond to release energy.

<p>Breaking bond to release energy.</p>
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Condensation Reactions

Reactions that build larger molecules.

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Active Transport

Movement of molecules against a gradient.

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Motor Proteins

Proteins that facilitate movement in cells.

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Molecular Motion

Random movement of atoms and molecules.

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Specificity of Enzymes

Enzymes bind only specific substrates.

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Energy Coupling

Using energy from exergonic reactions for endergonic.

<p>Using energy from exergonic reactions for endergonic.</p>
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Caloric Measurement

Energy changes measured in calories or joules.

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ΔH

Change in enthalpy during a reaction.

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ΔS

Change in entropy during a reaction.

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Temperature (T)

Factor affecting energy changes in reactions.

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Energy Loss

Occurs in reactions with negative ΔG.

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Enzyme

Biological catalyst speeding up chemical reactions.

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Active Site

Region on enzyme where substrate binds.

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Induced Fit

Enzyme shape change upon substrate binding.

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Reaction Rate

Speed at which reactants convert to products.

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Enzyme Occupancy

Maximum enzyme activity reached with substrate saturation.

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Activation Energy (EA)

Energy barrier that must be overcome for reaction.

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Inhibitors

Substances that decrease enzyme activity.

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Reversible Inhibitors

Non-covalently bind to enzymes, allowing recovery.

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Irreversible Inhibitors

Covalently bind, permanently disabling enzyme function.

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Allosteric Regulators

Bind away from active site, altering enzyme shape.

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Competitive Inhibitors

Compete with substrate for active site binding.

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Noncompetitive Inhibitors

Bind elsewhere, changing enzyme shape and function.

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Feedback Inhibition

Final product inhibits first enzyme in pathway.

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Phosphorylation

Addition of phosphate group to activate enzymes.

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Dephosphorylation

Removal of phosphate group to deactivate enzymes.

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Optimal pH

pH level where enzyme activity is maximized.

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Denaturation

Loss of enzyme structure, resulting in loss of function.

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Temperature Effect

Higher temperatures increase reaction rates to a point.

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DIPF

Irreversible inhibitor of acetylcholinesterase, a neurotoxin.

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Sarin

Nerve gas that irreversibly inhibits acetylcholinesterase.

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Malathion

Insecticide targeting insect enzymes specifically.

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Methotrexate

Anti-cancer drug that competitively inhibits purine synthesis.

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Enzyme Regulation

Control of enzyme activity through various mechanisms.

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Metabolic Pathways

Series of enzyme-catalyzed reactions in cells.

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Substrate Concentration

Amount of substrate available for enzyme activity.

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Kinetic Energy

Energy of motion affecting reaction rates.

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pH Measurement

Logarithmic scale measuring hydrogen ion concentration.

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Amino Acid R-groups

Side chains affecting enzyme structure and function.

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Cellular Control

Precise regulation of enzyme activity by cells.

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Enzyme Shape

Determined by amino acid interactions, crucial for function.

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Nerve Impulse

Signal transmission in neurons, requiring acetylcholinesterase.