2/26-3/3 Flashcards
Draw a mitochondrion and label each of the membranes, spaces,
o Explain the key differences in the outer and inner mitochondrial membranes and why
they have these differences**
https://www.purposegames.com/game/mitochondria-quiz
- Describe the flow of electrons from the primary electron carriers (NADH and FADH2) through the
electron-transport complexes, including cofactors, and state the purpose for each component in
the path (Figure 5.17 helps sum up)
- E- enter the chain from either NADH (via complex I) or FADH2 (a part of complex II).
- E- passed from either ubiquinone (UQ), which exists as a pool within the lipid bilayer, forming ubiquinol, to complex III and then to the peripheral protein cytochrome c, which is thought to be mobile.
- E- transferred from cytochrome c to complex IV (cytochrome oxidase) and then to O2 to make water.
- Explain the process of ATP synthase moving through the Loose -> Tight -> Open configurations
and how this is completed by the turning of the gamma stalk (ADD MORE DETAIL) ***
3 catalytic sites are in 3 different conformations- Loose-ADP + Pi are loosely bound, Tight- ADP + Pi are tightly bound, O- open, very low affinity for nucleotides, releases ADP and Pi. The turning of the Gamma stalk happens because the stalk connects both subunits. (The epilson subunit helps connect the stalk to the FO)
Structure of collagen
o Collagen**
Trimers consisting of three polypeptide chains (α chains).
wound around one another to form a rod-like triple helix. They contain large amounts of proline, and many of the proline (and lysine) residues are hydroxylated following synthesis of the polypeptide. The hydroxylated amino acids are important in maintaining the stability of the triple helix by forming hydrogen bonds between component chains
Structure of
o Proteoglycans****
-Core protein molecule (shown in black in Figure 7.9a) with chains of glycosaminoglycans (GAGs) are covalently attached (shown in red in the figure). (looks like a ladder E)
-Each GAG chain is a disaccharide
Structure of fibronectin
Linear array of building blocks (Sequence of ~30 Fn domains that make up 5/6 larger functional units)
Each of the two polypeptide chains that make up a fibronectin molecule contains the following:
Structure of Laminin****
-resembling a cross with three short arms and one long arm. Polypeptide chain
Outer membrane
-Serves as outer boundary for mitochondria
Inner membrane for mitochondria
Forms double membrane envelope and cristae. Also where TCA cycle and oxidative phosphorylation happens
Cristae-
The many deep folds in the inner mitochondrial membrane, which contain the molecular machinery of oxidative phosphorylation (aerobic respiration and atp formation- same or diff from ox phos?)
Matrix-
Aqueous compartments in interior of mitochondria
Cytosol-
where glycolysis takes place
o Explain the key differences in the outer and inner mitochondrial membranes and why
they have these differences**
Intermembrane space- Aqueous compartments between inner and outer membrane
Why do outer and inner membranes have these differences? Allow for different activities to take place
Outer- Has permeable porins which allow for ATP, NAD, CoA in, key roles for energy metabolism
Inner- Very impermeable (to retain their contents?)
No ribosomes, etc?
Structure of flavoproteins
polypeptide bound to flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN).
(Electron carrier) Cytochromes structures
proteins that have heme prosthetic groups
(Electron carrier) Three copper atoms- location
protein complex of the inner mitochondrial membrane
(Electron carrier) Ubiquinone (UQ, or coenzyme Q)- structure
long hydrophobic chain of five-carbon isoprenoid units
(Electron carrier) Iron-sulfur proteins- structure
proteinswith iron-sulfur center (Iron bound to inorganic sulfide). Most common centers have 2/4 atoms of iron and sulfur—designated [2Fe-2S] and [4Fe-4S]—linked to the protein at cysteine residues (Figure 5.13).
why electrons move through the molecules in ETC
Spontaneous reactions happen with a loss of free energy.
Collagen monomer, x-mer, sequences?
Monomer- a triple helix composed of three helical α chains. They’re trimers
What does collagen do?
-, creating mechanical properties of the matrix
How many types of collagen are there? Where are they found? Why is the number significant?
-28 types of collagen, found in tendon’s ECM, cornea, etc. Significant because they’re so variable.
How do proteoglycans’ structure create their function
form a porous, hydrated gel that fills the extracellular space like packing material. bind to a ton of cations, which bind to a ton of water molecules. Adjacent collagens make a strong scaffold, like in bone (which is hardened by calcium phosphate salts)
What do proteoglycans do?
Binding sites for components of the ECM, EG collagens, proteoglycans, and other fibronectin molecules. (Interconnect molecules). Enhanced by forces pulling on them and unfolding their components.
Laminin monomers/dimers/sequences
N/A
Laminin functions
Critical for cell migration, growth, and differentiation. (Like in the cells that give rise to sperm or eggs, from outside the embryo, moving to the gonads)
What can flavoproteins accept and donate
2 H+/e-.
Major mitochondrial flavoproteins
NADH dehydrogenase of the electron-transport chain and succinate dehydrogenase of the TCA cycle.
What can (Electron carrier) Cytochromes accept?
Can gain and lose one e-)
What types of (e- carrier) cytochromes are there in the ______? How are they differentiated?
A, B, C, ETC, Subs in the heme group
(Electron carrier) Three copper atoms- function
accept and donate a single electron as they alternate between the Cu2+ and Cu1+ states.
(Electron carrier) Ubiquinone (UQ, or coenzyme Q)- Can accept/donate what
2 e-/H+.
(Electron carrier) Ubiquinone (UQ, or coenzyme Q)- electronic state, and is the _____ of _____________
The partially reduced molecule is the free radical ubisemiquinone,
(Electron carrier) Ubiquinone (UQ, or coenzyme Q)- Fully reduced-
ubiquinol (UQH2).
Ubiquinol location and function-
lipid bilayer of the membrane, where it is capable of rapid lateral diffusion.
(Electron carrier) Iron-sulfur proteins- can accept and donate
1 e-.
(Electron carrier) Iron-sulfur proteins-Redox potential of an iron-sulfur center depends on
hydrophobicity /charge of the amino acid residues that make up its local environment.
(Electron carrier) Iron-sulfur proteins- potential
ranging from about −700mV to about +300mV, corresponding to a major portion of the span over which electron-transport occurs.
