Bioenergetics Flashcards

1
Q

Enenrgy

A

capacity of cause specific physical or chemical changes

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2
Q

Chemoheterotroph

A

human
carbon from organic compounds

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3
Q

Bioenergetic

A

subset of thermodynamics
how the biological world gain and use energy

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4
Q

1 molecule of glucose can couple with – of ATP molecules

A

30

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5
Q

chemotrophs

A

energy from oxidizing mebolic fuel

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6
Q

how many oxidizing state for carbon

A

5

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7
Q

most oxidizing state of carbon

A

CO2

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8
Q

1st law of thermodynamics

A

total energy universe remain the same

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9
Q

2nd law

A

universe always tend to greater randomness

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10
Q

measure of randomness

A

Entropy

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11
Q

Delta entropy universe is

A

positive for every spontaneous reaction

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12
Q

Enthalpy

A

heat content of a system

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13
Q

Gibbs free energy

A

dG=dH-TdS

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14
Q

Spontaneous reaction

A

dG negative
Exergonic
release free energy

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15
Q

nonspontaneous reaction

A

dG positive
Endergonic
Use free energy

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16
Q

system at equilibrium

A

dG zero
no net flow
enthalpy and entropy changes are exactly balanced

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17
Q

dG =

A

dG(0) + 2.303 RTK(eq)

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18
Q

Equilibrium constant

A

Reaction product conc. to reactant conc.

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19
Q

one way in biological pathway, making a reaction more favourable

A

constantly using product

20
Q

Homeostasis

A

Maintain a dynamic steady state far from equilibrium

21
Q

Speed of reaction and dG has – relation

22
Q

enzyme kinetic is based on

A

Activation energy

23
Q

all cellular processes are catalized by

A

enzyme or riboenzyme

24
Q

enzyme/riboenzyme properties

A

1- required in small amount
2- physiological temperature and pH
3- reusable
4- highly specific to their substrate
5- generate a specific product
6- they change the rate not dG

25
Metastable rate
thermodynamically unstable but does not have enough energy to exceed activation energy barrier
26
E(A)
minimum amount of energy required for reactant
27
Transition state
precise point when equal chance of going to product or substrate
28
How do enzymes reduce activation energy
1- maintaining precise substrate orientation 2- changiing substrate reactivity 3- exerting physical stress
29
active site
region enzyme that bind substrate and cofactor -complimentary pocket accommodate substrate with high affinity
30
amino acids comprise active site
C/S/D/E/H/K--SHDECK
31
water and enzyme active siute
water is generaslly excluded from active site if no treactant
32
metal and vitamins
use as enzyme and cofactor
33
rest of enzyme rather than active site
1- supopport structure 2- regulatory use 3- site of interaction with other proteins 4- substrate channel
34
eznymes are characterized by
sensivity to temperature and Ph
35
before optimal temp, enzyme activity increase when temperature
increases
36
after optimal temp, increase in temperature will
cause denaturation
37
pH dependence is due to
charged amino acids at active site ph change can disrupt ionic and HB bonds
38
rxn rate is influenced by
concentration of reactant/product/inhibitors
39
1pr 4domain VS 4pr 1domain
1pr 4domain one enzyme can regulate many reactions thisw\ way
40
cells can regulate protein activity by
localization turn them on/off
41
amount of enzyme can be regulated by
syntheis/degradation
42
drug and poisions normally
inhibit specific enzyme
43
competitive inhibition
inhibitor and substrate both bind to active site
44
noncompetetive inhibition
inhibitor bind difeerent than active sit, distort enzyme and inhibit substrate binding to active esite
45
allosteric regulation
bindign an effector molecule at a site rather than enzyme active site -common in multi subunit pr --can be inhibitor or activator
46
enzyme can be inactive/active until
activate/inactivate by covalent modification
47