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

A

no

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
Q

Metastable rate

A

thermodynamically unstable but does not have enough energy to exceed activation energy barrier

26
Q

E(A)

A

minimum amount of energy required for reactant

27
Q

Transition state

A

precise point when equal chance of going to product or substrate

28
Q

How do enzymes reduce activation energy

A

1- maintaining precise substrate orientation
2- changiing substrate reactivity
3- exerting physical stress

29
Q

active site

A

region enzyme that bind substrate and cofactor
-complimentary pocket accommodate substrate with high affinity

30
Q

amino acids comprise active site

A

C/S/D/E/H/K–SHDECK

31
Q

water and enzyme active siute

A

water is generaslly excluded from active site if no treactant

32
Q

metal and vitamins

A

use as enzyme and cofactor

33
Q

rest of enzyme rather than active site

A

1- supopport structure
2- regulatory use
3- site of interaction with other proteins
4- substrate channel

34
Q

eznymes are characterized by

A

sensivity to temperature and Ph

35
Q

before optimal temp, enzyme activity increase when temperature

A

increases

36
Q

after optimal temp, increase in temperature will

A

cause denaturation

37
Q

pH dependence is due to

A

charged amino acids at active site
ph change can disrupt ionic and HB bonds

38
Q

rxn rate is influenced by

A

concentration of reactant/product/inhibitors

39
Q

1pr 4domain VS 4pr 1domain

A

1pr 4domain
one enzyme can regulate many reactions thisw\ way

40
Q

cells can regulate protein activity by

A

localization
turn them on/off

41
Q

amount of enzyme can be regulated by

A

syntheis/degradation

42
Q

drug and poisions normally

A

inhibit specific enzyme

43
Q

competitive inhibition

A

inhibitor and substrate both bind to active site

44
Q

noncompetetive inhibition

A

inhibitor bind difeerent than active sit, distort enzyme and inhibit substrate binding to active esite

45
Q

allosteric regulation

A

bindign an effector molecule at a site rather than enzyme active site
-common in multi subunit pr
–can be inhibitor or activator

46
Q

enzyme can be inactive/active until

A

activate/inactivate by covalent modification

47
Q
A