Biochem and medical genetics
Help!
|
|
||||
|---|---|---|---|---|---|
| Mitochondrial structure | Double membrane
Relatively permeable outer membrane due to large porin channels
Highly impermeable inner membrane with highly specific transporters
Internal cristae structures to increase surface area
Internal matrix space
🗑
|
||||
| What do mitochondria contain enzymes for | ETC
TCA cycle
PDH
B oxidation
Ketone body metabolism
Urea cycle
Not all present in all mitochondria - tissue specific
🗑
|
||||
| Processes of oxidative phosphorylation | Couples two main processes
1 - generation of a proton gradients by oxidising H carriers, transporting electrons, consuming oxygen and producing water
2 - ATP synthesis using proton gradient to phosphorylate ADP
🗑
|
||||
| Chemiosmotic theory - Mitchell | Movement of electrons drives proton pumping
These protons are pumped from the matrix to the IMS
Creates electrical and pH gradient across the highly impermeable inner membrane
Protons move down gradient through ATP synthase
🗑
|
||||
| What is the ETC | 4 large complexes - each with many proteins
Complex 1 - 4
Linked by 2 small mobile electron carriers
Ubiquinone - Complex 1 and 2 to 3
Cytochrome C - Complex 3-4
🗑
|
||||
| What does the ETC need to transfer electrons | Oxidation/reduction reactions with increasing redox potential to pass electrons from NADH/FADH2 to O2
A way of facilitating single and double electron transfer
🗑
|
||||
| Types of groups used in electron transfer | Iron in Iron-sulphur clusters - complex 1, 2, 3
Iron as Haem in cytochromes - Complex 3 and 4 as well as cytochrome C
Copper - complex 4
🗑
|
||||
| Complex 1 | Uses HADH as substrate - freely diffusible in matrix
2 electrons pass through complex 1 to Flavin mono nucleotide, reducing it to FMH2, then to a series of FE-S clusters
Electrons to ubiquinone along with 2 H from matrix
Pumps 4 protons into IMS
🗑
|
||||
| Structure of Complex 1 | Transmembrane region involved in proton pumping
Matrix region involved in electron moving, oxidation of NADH and iron sulphur chain
🗑
|
||||
| Complex 2 | Uses FADH2 as substrate - physically linked to succinate dehydrogenase
2 electrons passed from FADH2 to a series of FE-S clusters
Electrons passed to Q along with 2 H from matrix
No proton pumping - not enough energy stored in FADH2
No communication
🗑
|
||||
| Ubiquinone | Known as Co-Enzyme Q10
Long hydrocarbon tail makes it highly hydrophobic
Retained in inner membrane, moving within the hydrophobic phospholipid environment
Can accept 2 electrons from complex 1 or 2 to produce QH2
🗑
|
||||
| Complex 3 | Uses Q as a substrate - produces 2 cytochrome C
Needs to accepts 2 electrons at once but release them one at a time without leaving electrons in the matrix unbound
contains 3 cytochromes, Rieske protein
Performs Q cycle
🗑
|
||||
| Q cycle | QH2 arrives - 1 electron to Rieske protein and straight to cytochrome C
Other binds to Cyt b and is transferred to Q to form a semi-quinone radical
Second QH2 binds - one electron to cytochrome C
Other to Cyt b then to the semi-quinone radical
🗑
|
||||
| Proton movement at complex 3 | Generates power to pump 4 protons into IMS
🗑
|
||||
| Cytochrome C | Transports 1 electron from complex 3 to 4
Water soluble, so resides at the periphery of membrane closer io intermembrane space
Contain haem prosthetic group
🗑
|
||||
| Complex 4 | Uses cytochrome C and O2 as substrates
Generates H2O
O2 is terminal electron acceptor
Electrons flow between haem and copper
O2 form peroxide bridge between terminal haem and copper
4 H pumped
🗑
|
||||
| Electron flow in complex 4 | 2 cytochrome C arrive - 1 electron to CuB and other to Haem a3
O2 forms peroxide bridge between them
Another 2 cyt C arrive - each donate an electron to the bridge
Addition of 2 protons forms OH groups
More protons form H2O
The products are halved
🗑
|
||||
| Structure of phosphorylation apparatus | Phosphate carrier
ATP synthase
ANT
Porins
🗑
|
||||
| Phosphorylation | The proton gradient is used to power a motor that phosphorylates ADP to ATP
The H gradient provides the intermediate that couples oxidation by ETC to phosphorylation
Done by ATP synthase
🗑
|
||||
| ATP synthase | Protons flow through F0 subunit - drives rotation of the y subunit via conformational changes
y subunit rotation drives F1 subunit conformational change that drive phosphorylation of ADP
🗑
|
||||
| F0 subunit | Protons enter through subunit a
Binds to aspartate residues in c subunit which neutralises the amino acids charge causing it to rotate
This drives rotation of y subunit
Linked to F1 portion
🗑
|
||||
| F1 subunit | B subunits catalyse ATP synthesis
Each is conformationally different - open, loose or tight
Open - ADP and Pi enter ATP leaves
Loose - held in place
Tight - synthesises ATP
Rotate between phases by y subunit rotation
🗑
|
||||
| Evidence - Boyer and Walker | Turned AT synthase upside down and attached to a membrane
Attached actin filament to y subunit
Cam visualise movement when proton gradient generated
🗑
|
||||
| Adenine nucleotide translocase and phosphate carrier | Use the proton gradient as well
Make the inside more positive by discharging electrochemical gradient
Take protons from ATP synthase
🗑
|
||||
| Evidence | Mitochondria alone and mitochondria with substrate consume little oxygen
Mitochondria only consume oxygen when stimulated by ADP which drives oxphos
Mitochondria stop consuming oxygen what all ADP is phosphorylated
Chemical inhibitors at any point
🗑
|
||||
| Thermogenesis | Occurs mostly in brown adipose tissue in newborn and hibernating animals
Uncoupling protein 1 expressed in these cells
Dissipates the proton gradient independently of ATP synthase, resulting in non-shivering heat generation
Uncouples oxphos
🗑
|
||||
| Dinitrophenol | A lipophilic weak acid that can cross the inner membrane and dissipate the proton gradient - chemical uncoupling
Electron transport and oxygen consumption continue uncontrolled but phosphorylation stops
Leads to hyperthermia etc
Cannot be reversed
🗑
|
||||
| AMP | Concentration usually 5nM
Adenylate kinase only forms this under insufficient ATP
Serves as an energy distress signal to the cell
Activates AMP activated protein kinase, which upregulates energy generating pathways and suppresses energy consumption
🗑
|
Review the information in the table. When you are ready to quiz yourself you can hide individual columns or the entire table. Then you can click on the empty cells to reveal the answer. Try to recall what will be displayed before clicking the empty cell.
To hide a column, click on the column name.
To hide the entire table, click on the "Hide All" button.
You may also shuffle the rows of the table by clicking on the "Shuffle" button.
Or sort by any of the columns using the down arrow next to any column heading.
If you know all the data on any row, you can temporarily remove it by tapping the trash can to the right of the row.
To hide a column, click on the column name.
To hide the entire table, click on the "Hide All" button.
You may also shuffle the rows of the table by clicking on the "Shuffle" button.
Or sort by any of the columns using the down arrow next to any column heading.
If you know all the data on any row, you can temporarily remove it by tapping the trash can to the right of the row.
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
Created by:
12345678987654321000000
Popular Medical sets