Spontaneous Generation Unit 3. What is Spontaneous Generation?
Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability,...
-
Upload
doris-henry -
Category
Documents
-
view
215 -
download
0
Transcript of Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability,...
![Page 1: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/1.jpg)
Figure 6.1 The complexity of metabolism
![Page 2: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/2.jpg)
Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change
![Page 3: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/3.jpg)
Figure 6.6 Energy changes in exergonic and endergonic reactions
![Page 4: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/4.jpg)
Figure 6.7 Disequilibrium and work in closed and open systems
![Page 5: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/5.jpg)
Figure 6.8 The structure and hydrolysis of ATP
![Page 6: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/6.jpg)
Figure 6.9 Energy coupling by phosphate transfer
![Page 7: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/7.jpg)
Figure 6.10 The ATP cycle
![Page 8: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/8.jpg)
Figure 6.11 Example of an enzyme-catalyzed reaction: Hydrolysis of sucrose
![Page 9: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/9.jpg)
Figure 6.12 Energy profile of an exergonic reaction
http://www.stolaf.edu/people/giannini/flashanimat/enzymes/transition%20state.swf
![Page 10: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/10.jpg)
Figure 6.13 Enzymes lower the barrier of activation energy
![Page 11: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/11.jpg)
Figure 6.14 The induced fit between an enzyme and its substrate
![Page 12: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/12.jpg)
Figure 6.15 The catalytic cycle of an enzyme
![Page 13: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/13.jpg)
Figure 6.16 Environmental factors affecting enzyme activity
![Page 14: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/14.jpg)
Characterizing enzymes
• Vmax - rate when enzyme is saturated with substrate
• KM – substrate concentration that allows reaction to proceed at 1/2 Vmax
• KM – useful as a measure of how tightly an enzyme binds its substrate– Low KM means tight binding, high KM
means weak binding
• Enzyme kinetics
![Page 15: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/15.jpg)
Characterizing enzymes
• Turnover number: Vmax/enzyme concen.
– typically about 1000 substrate molecules processed per second per enzyme molecule, but can be much higher
![Page 16: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/16.jpg)
Enzyme Turnover number (per second)
Carbonic anhydrase 600,000
Acetycholinesterase 25,000
Amylase 18,000
Penicillinase 2,000
DNA Polymerase 15
![Page 17: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/17.jpg)
Measuring enzyme activity
• One unit of an enzyme is defined as the amount that will catalyze a defined amount of substrate in one minute under specified conditions.
• For catalase:
one unit decomposes 1mole H2O2 at 250C at pH 7.
![Page 18: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/18.jpg)
What to measure for rate?
• Amount of substrate used over a specified time.
OR
• Amount of product accumulated over a specified time.
• Which to use???
![Page 19: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/19.jpg)
Figure 6.17 Inhibition of enzyme activity
![Page 20: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/20.jpg)
Figure 6.18 Allosteric regulation of enzyme activity
![Page 21: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/21.jpg)
Figure 6.19 Feedback inhibition
![Page 22: Figure 6.1 The complexity of metabolism. Figure 6.5 The relationship of free energy to stability, work capacity, and spontaneous change.](https://reader036.fdocuments.net/reader036/viewer/2022070415/56649ef45503460f94c06b36/html5/thumbnails/22.jpg)
Figure 6.20 Cooperativity