Biology 116 - Final Exam - Full Review Study Guide

Biology 116 - Final Exam - Full Review Study Guide From electron donor to electron acceptor (usually accompanied by protons H+) - Ans:-Electron transfer Electron carrier: Accepts two electrons plus one proton to form NADH - Ans:-NAD+ Electron carriers that readily accept or donate electrons - Ans:-Shuttles C and H have similar and form nonpolar bonds O and N have higher and tend to hog electrons - Ans:-Electronegativity Source of chemical energy - Ans:-Electrons Electron carrier: Access two electrons plus two Proteins to form FADH2 - Ans:-FAD Depends on Position of shared electrons and Distance from pos charges in nuclei. ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 2/211 Equally shared electrons have Higher potential energy than unequally shared electrons - Ans:-energy in covalent bonds the amount of disorder in a system. Entropy increases when organisedness decreases, energy released Entropy decreases when organisedness increases and energy just be spent to do that - Ans:-Entropy Total entropy always increases in a closed system. We are not a closed system due to sun. - Ans:- second law or thermodynamics where the substrate binds to the enzyme (usually via H-bonding) - Ans:-Active site Changes the conformation (shape) of the enzyme. Makes reaction more energetically favourable. - Ans:-induced fit Interactions between substrates and enzyme - Ans:-Transition state The energy input required for the reaction to proceed - Ans:-Activation energy ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 3/211 when temperature increases, concentration of substrate increases, enzymes have optimal temp and pH - Ans:-Reaction rate increases inorganic ions such as Zn 2+, Mg2+ and Fe2+ that reversible interact with enzymes (organisms require these minerals in diet) - Ans:-Cofactors Organic molecules like NADH or FADH2 that interact with enzymes (some are required in diet and called vitamins) - Ans:-Coenzymes Coenzymes permanently, covalently bound to enzymes - Ans:-prosthetic groups Form of energy used most often inside cells Unstable, most cells make it all the time by obtaining glucose through photosynthesis (plants) or from food - Ans:-ATP Animals store glucose as - Ans:-Glycogen Plants store glucose as - Ans:-Starch 1. Glycolysis 2. Pyruvate processing ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 4/211 3. Citric acid cycle 4. Electron transport and chemiosmosis - Ans:-4 steps of cellular respiration Pyruvate is oxidised to form Acetyl CoA - Ans:-Pyruvate processing Acetyl CoA is oxidised to CO2. - Ans:-Citrix acid cycle compounds that were reduced in steps 1-3 are oxidized in reactions leading to ATP production - Ans:- Electron transport and chemiosmosis Glucose (6) is broken down to pyrovate (2x3) occurs in cytoplasm . Glucose split in half, each half is phosphorylated, 2 ATP spent - Ans:-Glycolysis ATP is made by transferring a phosphate directly from an intermediate substrate to ATP - Ans:- substrate-level phosphorylation In step 4, a proton gradient provides energy for ATP production, membrane protein ATO synthase uses this energy to phosphorylate ADP to form ATP - Ans:-Oxidative ohosphorylation Occurs in every prokaryote and eukaryotes group) regulated by controlling production or activation of enzymes. Spend 2 ATP, end gives you 4 ATP. Net of 2 ATP produced. - Ans:-Glycolysis summary Cause breakdowns of molecules, can harvest stored chemical energy to produce ATP - Ans:-Catabolic pathways ©GRACEAMELIA 2024/2025 ACADEMIC YEAR. ALL RIGHTS RESERVED FIRST PUBLISH OCTOBER 2024 Page 5/211 Result in the synthesis of larger molecules from smaller components Often use energy in the form of ATP. - Ans:-Anabolic pathways Cells will first use carbohydrates, then fats, then proteins - Ans:-Fasting Mitochondria of eukaryotes - Ans:-Steps 2 -3 occur in Enzyme complex. ATPase 'knob' (F1 unit)