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Microbiology Test 1 > Chapter 4 - PPT > Flashcards

Chapter 4 - PPT Flashcards

(61 cards)

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1
Q

Metabolism

A

–The sum total of all chemical reactions that occur in a cell

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2
Q

Catabolic Reactions

A

Energy-releasing metabolic reactions

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3
Q

Anabolic Reactions

A

–Energy-requiring metabolic reactions

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4
Q

Nutrients

A

Supply of monomers (or precursors of) required by cells for growth

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5
Q

Macronutrients

A

Nutrients required in large amounts

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6
Q

Essential Elements by Dry Weight in Cell

A
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7
Q

Macromolecular Composition of a Cell

A
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8
Q

Growth Factors

A

Organic compounds required in small amounts by certain organisms
Examples: vitamins, amino acids, purines, pyrimidines
Vitamins
Most commonly required growth factors
Most function as coenyzmes

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9
Q

Culture media

A

Nutrient solutions used to grow microbes in the laboratory

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10
Q

Defined media:

A

precise chemical composition is known

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11
Q

Complex media:

A

composed of digests of chemically undefined substances (e.g., yeast and meat extracts)

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12
Q

Selective Media

A

Contains compounds that selectively inhibit growth of some microbes but not others
IF it grows or not

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13
Q

Differential Media

A

Contains an indicator, usually a dye, that detects particular chemical reactions occurring during growth
HOW it grows in comparison

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14
Q

Pure culture:

A

culture containing only a single kind of microbe

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15
Q

Free energy (G):

A

energy released that is available to do work

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16
Q

Exergonic reactions

A

Negative deltaG0′
Release free energy

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17
Q

Endergonic reactions

A

Positive DeltaG0′
Require energy

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18
Q

Activation energy:

A

energy required to bring all molecules in a chemical reaction into the reactive state
A catalysis is usually required to breach activation energy barrier

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19
Q

Activation energy with and without catalyst

A

Red no enzyme

Green with enzyme

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20
Q

Catalyst:

A

substance that
Lowers the activation energy of a reaction
Increases reaction rate
Does not affect energetics or equilibrium of a reaction
Are not consumed or transformed by reaction

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21
Q
A
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22
Q

Enzymes

A

Biological catalysts
Typically proteins (some RNAs)
Highly specific
Function of 3D structure
Typically rely on weak bonds
Examples: hydrogen bonds, van der Waals forces, hydrophobic interactions
Active site: region of enzyme that binds substrate

Increase the rate of chemical reactions by 108 to 1020 times the spontaneous rate
Enzyme catalysis: E + S E  S E + P
Catalysis dependent on
Substrate binding
Position of substrate relative to catalytically active amino acids in active site

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23
Q

E+SE-SE+P

A
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24
Q

Oxidation:

A

the removal of electron(s)

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25
Reduction:
that addition of electron(s)
26
Electron donor:
is oxidized in a redox reaction
27
Electron acceptor:
is reduced in a redox reaction
28
Picture an electron moving in a redox reaction
29
Picture an electron moving in a redox reaction
30
Reduction potential (E0′):
tendency to donate electrons Expressed as volts (V) The reduced substance at the top of the tower donates electrons
31
Redox tower
32
ΔE0’
Energy released Difference is reduction potential between donor and acceptor redox couple The further electrons “drop” from a donor before they are “caught” by an acceptor the greater the amount of energy Proportional to ΔG0’
33
Long-term energy storage involves insoluble polymers that can be oxidized to generate ATP What is used in Bacteria and Archea? What is used in Eukaryotes
Bacteria and Archaea Glycogen Poly--hydroxybutyrate and other polyhydroxyalkanoates Elemental sulfur Eukaryotes Polyglucose Starch Lipids (simple fats)
34
Electron Transport System
Membrane associated Mediate transfer of electrons Conserve some of the energy released during transfer and use it to synthesize ATP Many oxidation–reduction enzymes are involved in electron transport e.g., NADH dehydrogenases, flavoproteins, iron–sulfur proteins, cytochromes
35
What are the parts involved with the Electron Transport chain?
36
NADH dehydrogenases:
Proteins bound to inside surface of cytoplasmic membrane Active site binds NADH and accepts 2 electrons and 2 protons that are both passed to flavoproteins e- AND H+
37
Flavoproteins
Contains flavin prosthetic group (e.g., FMN, FAD) Accepts 2 electrons and 2 protons but only donates the electrons to the next protein in the chain
38
Cytochromes
Proteins that contain heme (iron) prosthetic groups Accepts and donates a single electron via the iron atom in heme (iron)
39
Quinones
Hydrophobic non-protein-containing molecules Participate in electron transport chain Accept electrons and protons but pass along electrons only
40
Whata are the complexes of the electron transport chain, and what do they do?
Complex I NADH is oxidized and e- added to quinone pool ( is reduced) Complex II Bypasses complex I and feeds e- and H+ from FADH to quinone pool Complex III e- passed from quinone pool to cytochrome b-c1 complex e- passed to cytochrome c – an e- shuttle Complex IV e- passed to cytochromes a and a3 Terminal oxidase – adds e- to terminal electron acceptor (i.e. O2)
41
Visualize the Electron transport chain, and complexes. What is the change in Eo'
42
How many protons come off in the electron transport chain and why?
43
Image of electron transport chain used one quiz
44
Proton Motive Force
The inside becomes electrically negative and alkaline The outside becomes electrically positive and acidic
45
ATP synthase (ATPase):
Complex that converts proton motive force into ATP Two components : F1: multiprotein extramembrane complex, faces cytoplasm Fo: proton-conducting intramembrane channel F1 and F0 are rotary motors Reversible to generate proton motive force by using ATP Norm dissipates proton motive force and makes ATP
46
Visualize the ATP Synthase
47
Respiration:
ATP produced from proton motive force formed by transport of electrons
48
Aerobic Respiration
O2 is the terminal electron acceptor
49
Anaerobic Respiration
Alternative element as the terminal electron acceptor NO3-, NO2-, Fe3+, SO42-, CO32- Redox tower
50
Chemoorganotrophy, Breakdown, What goes in, what comes out...
51
What is the terminal electron accetor in Anaerobic respiration?
NO3-
52
Chemoorganotrophs Respiration
Oxidative phosphorylation ATP produced from proton motive force formed by transport of electrons
53
Fermentation:
Substrate-level phosphorylation ATP directly synthesized from an energy-rich intermediate
54
Fermentation products of Glycolosis
55
Chemolithotrophy
Uses inorganic chemicals as electron donors Examples include hydrogen sulfide (H2S), hydrogen gas (H2), ferrous iron (Fe2+), ammonia (NH3) Typically aerobic Begins with oxidation of inorganic electron donor Uses electron transport chain and proton motive force Autotrophic; uses CO2 as carbon source
56
Breakdown of Chemolithotrophy, Products,
57
Phototrophy
uses light as energy source
58
Photophosphorylation:
light-mediated ATP synthesis
59
Photoautotrophs
use ATP for assimilation of CO2 for biosynthesis
60
Photoheterotrophs:
use ATP for assimilation of organic carbon for biosynthesis
61
Breakdown of Phototrophs

Microbiology Test 1 (6 decks)

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