Exam 2 Flashcards
vocabulary (30 cards)
Carbohydrate
Aldehydes or ketone with at least two hydroxyl groups or substances that yield such compounds upon hydrolysis
- most abundant biomolecules in nature
Stereoisomer
two or more compounds with the same molecular formula different only in spatial arrangement of their atoms.
Enantiomer
(optical isomer) stereoisomers that are mirror images
Diastereomers
stereoisomers that are not enantiomers (not mirror images)
Epimer
one of two stereoisomers that differ in configuration at only one stereocenter. ( an anomer is a type of epimer)
Aldose
sugar with the carbonyl group at the end of the carbon chain ( in aldehyde group)
Hemiacetal (/hemiketal)
Hemiacetal(ring formations) -
an alcohol and ether attached to the same carbon.
Ketose
sugar with the carbonyl group anywhere but the ends
acetal (/ketal)
hemiacetals and hemiketals react with alcohols to form the corresponding acetal and ketal
Pyranose
six-membered rings
Furanose
five-membered rings
Anomer (a and b)
two possible diastereomers that form because of cyclization
Substrate-level phosphorylation
the direct formation of ATP or GTP by transferring a phosphate group from a high-energy compound to an ADP or GDP molecule (in cytoplast or mitochondria)
The Chemiosmotic Theory
- As electrons pass through the ETC, protons are pumped into the intermembrane space from the matrix, generating an electrical potential and a proton gradient (protonmotive force)
- Protons move back across the inner membrane to the matrix (down their concentration gradient) through ATP synthase, driving ATP formation
According to the Chemiosmotic Theory, ATP synthesis in mitochondria is driven by
Membrane potential and gradient
ATP synthesis
Requires translocation of three protons through the ATP synthase
ATP synthase consists of two rotors – F1 unit (the ATP synthase) and F0 unit (transmembrane channel) – linked by a strong flexible stator
ATP synthase steps
Steps:
1. ADP and Pi bind to L site; rotation converts it to T conformation
2. ATP synthesized
3. Rotation converts T site to O site, releasing ATP
F0 motor role
F0 motor converts the protonmotive force into the rotational force of the central shaft which drives ATP synthesis
Oxidative phosphorylation
Activated when ADP (respiratory control) and Pi concentrations are high
Inhibited when ATP concentrations are high
Amounts of ATP and ADP in mitochondria are
controlled by the ADP-ATP translocator
What type of reactions are NAD and NADP involved in?
Two coenzyme forms: nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP)
Have oxidized (NAD+ and NADP+) and reduced (NADH and NADPH) forms
NAD+ is involved in catabolic reactions and NADP+ is involved in biosynthetic reactions
Redox reactions - roles of coenzymes
Living organisms utilize redox coenzymes as high-energy electron carriers (e.g., NADH and FADH2) from nicotinic acid and riboflavin vitamin molecules
What is FAD and its function?
Riboflavin (vitamin B2) is a component of two coenzymes: flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD)
-Function as dehydrogenases, oxidases, and hydroxylases
Coenzyme A
Coenzyme A (CoA) is an acyl carrier molecule
- Because the reactive SH group forms a thioester bond with acyl groups, coenzyme A is often abbreviated as CoASH
ETC purpose
is a mechanism by which electrons are transferred from NADH and FADH2 to a series of electron carriers, arranged in order of increasing electron affinity, that are sequentially reduced and then oxidized