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chapter 11 Flashcards

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1
Q

metabolism

A

the complete set of chemical reactions that allow cells to grow and devide

metabolic pathways

metabolites

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2
Q

metabolic pathways

A

series of enzyme-catalyzed rxns

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3
Q

metabolites

A

(metabolic intermediates)

the chemical intermediates
-substrates, intermediates, products

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4
Q

what are the chemical intermediates

A

substrates

intermediates

products

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5
Q

all pathways share the same-

A

fundamental chemical and thermodynamic principles

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6
Q

catabolism

A

to degrade compounds for usable energy (and obtain ‘simple’ components)

oxidative

cofactors are reduced (oxidizing agents)

-NAD+, FAD, NADP+

-electrons primarily destined for the ETC

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7
Q

oxidative

A

bonds broken (loss of electrons

provides energy

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8
Q

anabolism

A

to synthesize compounds needed to live/grow from ‘simple’ components

reductive

cofactors are oxidized (reducing agents) - NADPH, NADH

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9
Q

reductive

A

bonds formed (gain of electrons)

requires energy

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10
Q

purpose of metabolism

A

catabolism and anabolism

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11
Q

virtually all chemical reactions are-

A

enzyme catalyzed

-would not otherwise proceed at rates needed within the cell

-control of individual reactions and overall metabolic pathways

-efficiency- stereospecificity reduces ‘waste’

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12
Q

types of reactions

A

oxidations and reductions

group transfers

isomerizations, rearrangements

make/break C-C bonds

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13
Q

oxidations and reductions

A

transfer or elections (oxidoreductases)

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14
Q

group transfers

A

transfer of final groups (transferases, hydrolases)

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15
Q

isomerizations,rearrangements

A

same atoms, differnt arrangement

(isomerases, mutases)

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16
Q

make/break C-C bonds

A

they make or break C-C bonds

(hydrolases, ligases, lyases

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17
Q

diatary macromolecules

A

nucleic acids

proteins

polysaccharides (complex carbohydrates)

triacylglycerols (fats)

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18
Q

nucleic acids

A

nucleotides

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19
Q

proteins

A

nucleotides

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20
Q

polysaccharides

A

monosaccharides (simple sugars)

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21
Q

triacyglycerols

A

fatty acids

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22
Q

what dietary macromolecule is not a significant fuel source

A

nucleic acids

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23
Q

what dietary macromolecule is the most significant fuel sources

A

polysaccharides

triacyglycerols

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24
Q

Excess fuel storage: carbohydrates are stored as-

A

glycogen

-in the liver (heptocytes)

-in the skeletal muscle (myocytes)

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25
glycogen
a polymer of glucose molecules
26
excess fuel storage: fatty acids are stored as-
fat (triacylglycerols) in adipocytes
27
bioenergrtics
the quantitive study of energy relastionships and interconvertions in biological systems
28
thermodynamics applies to-
all metabolic reactions -metabolic pathwayds and enzyme catalyzed reactions due NOT circumvent this
29
What is G
free energy: G= H-TS
30
what is ^G
change in free energy
31
what is H
enthalpy
32
What is S
entropy, randomness in a system
33
enthaply
total content of heat of a system
34
entropy
a measure of the number of ways a system can be arranged
35
what is the thermodynamic equation
^G = Gp - Gr = ^H - T^S
36
if ^G is negative,
the reaction will proceed spontaneously in the forward direction
37
if ^G is positive
the reaction will not proceed spontaneously in the forward direction
38
a reaction will only proceed in the forwards direction when the associated value of ^G is-
negative (<0)
39
^G gives what info on rate of reaction?
NONE
40
^G > 0
reaction will not occur (in the forward direction ) A -x-> B
41
^G < 0
A --> B reaction will occur (sponetaneous)
42
^G ~ 0
A <---> B reaction considered 'reversibe'
43
^G provides info regarding
the driving force to achieve equilibrium -sense of direction and magnitude -does not provide any info regarding the mechanism or the rate for the reaction A<--->B ^G = +
44
^Go is a constant directly related to the
equilibrium constant (Keq) under standard conditions
45
what is standard conditions
101.3 kpa, 298k, 1 M
46
^G in any condition is a function of
the standard free energy change ^Go
47
biological systems under typical cellular conditions
use the transformed standard constants ^Go and Keq
48
standard condition equation
^Go = -RT in (keq)
49
^G function of standard free energy change equation
^G = ^Go + RT In [C]c[D]d/[A]a[B]b
50
free energy changes
A+B <--keq---> C+D
51
biochemical standard state conditions equations
^Go = Gop - Gor = ^H -T^S Keq = [C][D]/[A][B] ^Go = -RT InKeq
52
^Go and Keq are
constant for a given reaction
53
^Go = -RT InKeq measures of spontaneity : Keq = >1 and ^Go = -
spontaneous (proceeds forward)
54
^Go = -RT InKeq measures of spontaneity: Keq = 1.0 ^Go = 0
at equilibrium
55
^Go = -RT InKeq measures of spontaneity: Keq = <1 and ^Go = +
non-spontaneous (proceeds in reverse)
56
actual free energy changes depend on the-
reactant and product concentrations (and tempertaures)
57
The ^G determines if a-
reaction proceeds or not NOT THE ^Go ^G is a function of ^Go [products],[substrates], and temperture
58
a reaction with a + ^Go may have a
negative ^G, under cellular conditions
59
^G can be determined under non-equilibrium conditions if we know the
[ ] or ratios of products and reactants
60
energy coupling
another method to overcome unfavourable reactions the additive standard free energy change associated with sequential reactions (elementary or overall) sharing a common intermediate
61
energy released by exergonic reaction can-
drive the endergonic reactions -free energy changes of reactions are additive
62
the free energy change of coupled reactions are-
additive
63
high energy intermediates are
compounds which contain 'usuable chemical energy -energy can be recovered or used
64
what are the three types of high energy intermediates
nucleotide triphosphates thioesters electron carriers
65
nucleotide triphosphates
NTPs: ATP, GTP, UTP, CTP -addiontional : phosphocreatine and phosphoenolpyruvate (PEP)
66
what are NTPS
ATP GTP UTP CTP
67
electron carriers
NADH, NADPH, FADH2, FMNH2 coenzymes that serve as electron carriers (not high energy)
68
ATP hydrolysis yields an enormous amount of energy per mole due to:
- the relief of charge repulsion -resonance stabilization of released Pi -solvation energy difference
69
Adenosine Triphosphate (ATP_
energy currency generated by catabolism
70
energy currency
common in muiltple systems phosphanhydride bond makes it 'high' - energy
71
generated by catabolism ATP
ATP is generated directly through breakdown of sugar molecules and by via reoxidation of NADH/FADH2 by ETC (~90%)
72
what is ATP used in?
driving unfavourable reactions (coupling) movement (muscle, flagella) primary active transport (ion pumping)
73
ATP typically provides energy by-
group transfer reactions
74
free energies of hydrolysis for phosphate-containing compounds can be referred to as the-
phosphate transfer potential Measure of energy stored in phosphate bonds before broken and energy that is released or transferred when those bonds are broken
75
^G of phosphate hydrolysis from ATP is
intermediate ATP can act as a Pi donor ATP can be synthesized by Pi transfer
76
why doesnt ATP undergo spontaneous hydrolysis?
Thermodynamics kinetics
77
why doesnt ATP undergo spontaneous hydrolysis? Thermodynamics
-high energy bond hydrolysis is energetically favourable -> spontanouse rxn
78
why doesnt ATP undergo spontaneous hydrolysis? kinetics
-large activation energy barrier with hydrolysis of high-energy bonds -very slow rate without an enzyme catalyst results in kinetic sability
79
kinetic stability is essential for energy storage molecules
-rapid ATP hydrolysis without catalyst would render ATP useless for energy storage -allows for ATP hydrolysis only when coupled to a useful cellular rxn
80
principles of electrochemisty
when descirbing electron trasfers, the oxidation and reduction halves of the reaction can be considered separatly overall rxn: Fe2+ + Cu2+ <--> Fe3+ + Cu+ Half rxns: oxidation of ferrous ion (loss of an e-) Fe2+ (red) <--> Fe3+ (oxi) + e- reduction of cupric ion (addition of e-) Cu2+ (oxi) + e- <--> Cu+ (red)
81
what is reduction potential
a measure of the affinity for electrons
82
reduction potential of a half cell depends on
concentrations / activities of the chemical species present
83
oxidation potentials
the electrochemical potential for oxidation half rxns has the same magnitude but opposite sign reverse of written rxns (right)
84
The flow of electrons makes energy-
available
85
the free-energy change of a redox reaction equation
^G = -n F ^E or ^Go = -n F ^Eo
86
nucleotides play another central role in metabolism as
electron carriers energy can be recovered or used
87
what is NAD+
Nicotinamide Adenine Dinucleotide
88
What is NADP+
Nicotinamide Adenine Dinucleotide Phosphate
89
What is FAD
Flavin Adenine Dinucleotide
90
NAD+, NADP+, FAD are-
all cofactors FAD is a prosthetic group of NAD+/NADP+ are co-substrates The nitrogen base portion enables them to undergo a reversible reduction reactions (gain electrons)
91
each individual reaction obeys thermodynamic laws:
-free energy change must be - (^G <0) to proceed ^G = ^Go + RTIn ([products]/[reactants])
92
a series of enzyme-catalyzed chemical reactions: ^G neg is
-irreversible -enzyme "slow" -insufficient catalytic activity -enzyme regulated -rate limiting -can be reversed by increasing [B]
93
a series of enzyme-catalyzed chemical reactions: ^G ~ 0 is
reversible enzyme "on" rate driven by [C] and [D]
94
irreverible steps are
usually regulated
95
reversible steps are-
not usually regulated
96
rate-limiting steps
in a pathway, are the irreversible, regulated reactions -determine the overall rate
97
product inhibition
an enzyme is inhibited by the product of its reaction
98
feedback inhibition
an enzyme is inhibited by a metabolite further down the pathway
99
activation
an enzyme may be activated by a metabolite "upstream" -ensures that the pathway is funtioning in concert -feed-forward activation
100
competing metabolic pathways
-competing pathways must have differntial processes free energy problem (catabolic vs anabolic) independent routes allows for differential control of each pathway

biochem (9 decks)

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