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the amount of energy that is available to do work |
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energy that is associated with position or configuration |
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first law of thermodynamics |
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energy is conserved; energy cannot be created or destroyed, but only transferred & transformed |
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the total energy in a molecule (represented by H) |
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when a reaction releases heat energy (products have less potential energy than the reactants); deltaH is negative |
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if heat energy is taken up during the reaction, generating products that have higher potential energy than the reactants; deltaH is positive |
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amount of disorder (symbolized by deltaS) |
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second law of thermodynamics |
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total entropy always increases in an isolated system |
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deltaG = deltaH - T(deltaS) |
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spontaneous reactions; deltaG < 0 |
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nonspontaneous reactions; deltaG > 0 |
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effect of concentration of reactants on number of collisions occurring between substances in a mixture |
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high concentration = more collisions (faster reactions) |
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effect of temperature on number of collisions occurring between substances in a mixture |
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high temperature = more collisions (faster reactions) |
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between exergonic & endergonic reactions, chemical energy released from one reaction drives another |
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reduction-oxidation reactions (redox reactions) |
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chemical reactions that involve the loss or gain of one or more electrons |
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the atom in one molecule from which electrons may be transferred |
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the atom in one molecule to which electrons may be transferred |
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flavin adenine dinucleotide (FAD) |
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Definition
a cellular electron acceptor that is reduced by two electrons accompanied by two protons to form FADH2 which then donates the high-energy electrons to other molecules |
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a molecule that first accepts protons & electrons & then donates the electrons to other molecules |
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nicotinamide adenine dinucleotide (NAD+) |
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Definition
common molecule that first accepts protons & electrons & then donates the electrons to other molecules |
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adenosine triphosphate (ATP) |
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makes things happen in cells because it has a great deal of potential energy |
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raises 1 kilogram (kg) or water 1 degree C |
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target molecule to which the cleaved phosphate from ATP hydrolyzation is transferred |
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the addition of a phosphate group to a substrate |
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the substrate binding site in enzymes in which substrate molecules are brought together |
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many enzymes undergo a significant change in shape (conformation) when reactant molecules bind to the active site |
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a temporary, unstable, intermediate condition between the substrate & enzyme |
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the certain amount of kinetic energy required to strain the chemical bonds in substrates so they can achieve the transition state |
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1. initiation 2. transition state facilitation 3. termination |
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initiation step of enzyme action (1) |
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Definition
reactants bind to the active site in a specific orientation, forming an enzyme-substrate complex |
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transition state facilitation step of enzyme action (2) |
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Definition
interactions between enzyme & substrate lower the activation energy required |
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termination step of enzyme action (3) |
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Definition
products have lower affinity for active site & are released; enzyme is unchanged after the reaction |
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effect of increase in substrate concentration from low substrate concentrations on speed of an enzyme-catalyzed reaction |
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Definition
increase in steep, linear fashion |
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effect of increase in substrate concentration from intermediate substrate concentrations on speed of an enzyme-catalyzed reaction |
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Definition
increase in speed begins to slow |
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effect of increase in substrate concentration from high substrate concentrations on speed of an enzyme-catalyzed reaction |
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reaction rate plateaus at maximum speed |
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3 types of enzyme "helpers" |
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Definition
1. cofactors 2. coenzymes 3. prosthetic groups |
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inorganic ions, such as the metal ions Zn2+ (zinc), Mg2+ (magnesium), & Fe2+ (iron), which reversibly interact with enzymes |
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organic molecules that reversibly interact with enzymes, such as the electron carriers NADH or FADH2 |
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non-amino acid atoms or molecules that are permanently attached to proteins, such as the molecule retinal |
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2 ways that reversible modifications affect enzyme function |
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Definition
1. the regulatory molecule is similar in size & shape to the enzyme's natural substrate & inhibits catalysis by binding to the enzyme's active site 2. the regulatory molecule binds at a location other than the active site & changes the shape of the enzyme |
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Definition
the substrates cannot bind when a regulatory molecule binds to the enzyme's active site |
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the active site becomes available/unavailable to the substrates when a regulatory molecule binds to a different site on the enzyme |
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Definition
a series of reactions, each catalyzed by a different enzyme, that builds the molecules of life |
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when an enzyme in a pathway is inhibited by the product of the reaction sequence |
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3 steps of the retro-evolution hypothesis |
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Definition
1. enzyme 1 evolves to convert substrate 1 into a key produce involved in chemical evolution 2. substrate 1 is used up & a new enzymatic activity evolves to produce substrate 1 from another substrate 3. the cycle repeats |
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a new technology that scrutinizes & engineers the metabolic activity of microbes to clean up a variety of human-made pollutants |
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those that break down molecules for sources of energy & carbon building blocks |
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those that use energy & carbon building blocks to synthesize molecules |
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