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Week 12 Notes

by: Jordana Baraad

Week 12 Notes BSC 450

Jordana Baraad
GPA 3.9

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About this Document

Attached are notes from this week, which due to Thursday's test, are intended to accompany the powerpoint from Tuesday 11/10
Fundamentals of Biochemistry
Dr. Ramonell
Class Notes
25 ?




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This 3 page Class Notes was uploaded by Jordana Baraad on Saturday November 14, 2015. The Class Notes belongs to BSC 450 at University of Alabama - Tuscaloosa taught by Dr. Ramonell in Summer 2015. Since its upload, it has received 41 views. For similar materials see Fundamentals of Biochemistry in Biological Sciences at University of Alabama - Tuscaloosa.

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Date Created: 11/14/15
BSC 450 Direct C-C… Stabilize carbanions in C-C bond cleavage / formation Carbonyl group somewhere on molecule Stabilize through resonance Carbonyl Compounds 2 main rxns for forming C-C bonds aldol by far most common key intermediate: enolage run in reverse = aldolase – break C-C bond glycolysis: rearranging –OH’s & carbonyls Decarboxylations Common, also fromm enolate intermediate Seen in series in Citric Acid Cycle Breaks C-C bond Key: position of –OH’s & carbonyls Rearrangement Isomerization & Elimination Goal: correct placement function groups In-detail (later): glucose-6-phosphate  fructose-6-phosphate Phase 1 glycolysis Sets up to split  G3P & DHAP Proper cleavage Intermediate: enediol Often coupled w/ decarboxylation st Needs groups in right spot 1 Free Radical Rxns Not covered Key: well-controlled Radical on enzyme Complete control of where/when radical formed Typically, Tyr used Rxn pictured  decarboxylation Group Transfer Rxns 1. phosphate transfer: most common a. sometimes direct donations i. ex. glycolysis: high-energy molecules donate to ATP b. add phosphate group: kinases c. remove phosphate group: phosphates 2. acyl group transfer 3. glycosyl group Oxy-Redox Rxns Pic: most reduced  least reduced / most oxidized Most reactions we look at have –OH groups Ex. sugar reduction Reduction to lowest energy form: CO2 Done by pulling electrons Must be accepted immediately Need electron carriers NAD, NADP, FAD, FMN: create proton gradient  lots of indirect ATP synthesis stepwise rxns (controlled) Multiple Ways for Electrons… 1. single electron transfers a. metal ions (Mg , Cu) 2. rxn w/ oxygen Biological Oxidation Reduction major class: dehydrogenases—large enzymes precipitate succinate dehydrogenate in Citric Accid Cycle NAD = cofactor Part of fermentation In absence of O2 If can’t go Citric Acid Cycle, replenish NAD to perpetuate glycolysis Transfer electrons back NAD+ & NADP are coenzymes all derived from Niacin (Vitamin B3) B Vitamins important to keep energy up Adenosine residue Large; lots of favorable interactions With enzyme possible Rossman-Fold: pink “business end” Nicatinamide ring (in both) 2 electron carriers picks up 2 protons to balance most enzymes prefer A configuration H+ pointing out—available NAD+ & NADPH mostly involved in catabolic rxns—electron donors NADPH in photosynthesis NADH v. flavins NADH 2 electrons more flexible 1 acceptor = flavin Fe-S cluster Accepts electron at a time Transient bond Flavins 1 or 2 electrons donaes FADH  succinate dehydrogenate permanent; attached in enzyme site FAD & FMN Derived from riboflavin (Vitamin B2) Adenine—huge structure  favorable binding “business end” : ring 3 ring structure takes 1 electron at a time 1 electron transfer  semiquinone 2 electron transfer  full reduction FADH 2 Permanent attachment Must be able to reset


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