Biochemistry And Cellular Respiration Flashcards
Second law of thermodynamics
Disorder or entropy tends to increase
First law of thermodynamics
Law of conservation of energy
Symbol for entropy
S
Symbol for free energy (Gibbs)
G
Symbol for enthalpy
H
Gibbs free energy - equation
Delta-G = Delta-H - T*Delta-S
What are proteases?
Protein cleaving enzymes
What are the four main ways enzyme activity is regulated?
- Covalent modification (i.e.- phosphorylation of a site can activate OR deactivate)
- Proteolytic cleavage - synthesized inactive, cleaved by protease to activate
- Association with other polypeptides (i.e.- regulatory subunit slows down activity)
- Allosteric regulation - modification of active site via interactions in the allosteric site
Enzyme Cooperativity
The binding of one substrate molecule to the enzyme complex enhances the binding of more substrate molecules to the same complex
(*these enzymes must have more than one active site)
Competitive inhibition
Molecular inhibitors compete with substrate at active site
Noncompetitive inhibition
Molecular inhibitors bind at allosteric site
4 Stages in Cellular Respiration
- Glycolysis
- PDC (pyruvate dehydrogenase complex)
- Krebs Cycle (or citric acid cycle)
- Electron transport chain
Basic In’s & Out’s of Glycolysis
Glucose + 2ADP + 2P-i + 2NAD(+)
➡️➡️➡️
2 Pyruvate + 2ATP + 2NADH + 2H2O + 2 H(+)
Hexokinase
Enzyme that catalyzes first step in glycolysis (phosphorylation of glucose to G6P)
Phosphofructokinase (PFK)
Catalyzes third step in glycolysis - Important bc extremely favorable reaction- practically irreversible (a committed step)
Basic in’s & out’s of PDC
Pyruvate + CoA-SH + NAD(+)
➡️➡️➡️(oxidation of pyruvate)
Acetyl-CoA + NADH + H(+) + CO2
Coenzyme-A
(CoA-SH) - Coenzyme used in many reactions to pass acetyl units around - Plays major role in PDC
Describe what happens in PDC
- Pyruvate transported for. Cytoplasm to inner Mitochondrial matrix
- Here it is oxidative lay decarboxylated by the pyruvate dehydrogenase complex, which is composed of three different enzymes (allows intermediates to be passed from active site to active site)
Prosthetic groups vs Co-factors
Prosthetic group - a no protein molecule covalent.y bound to an enzyme at it’s active site
Co-factor - various organic and inorganic substances necessary to enzyme function but which never actually interacts with the enzyme
Basic Ins and Outs of the Krebs Cycle
Acetyl-CoA + OAA + 3NAD(+) + FAD + GDP
➡️➡️➡️➡️
2-CO2 + OAA + 3 NADH + FADH2 + GTP
Describe what happens in Krebs Cycle
First step: Actyl-CoA (2C) + Oxaloacetate (4C) forms intermediate of citrate (CoA-SH regenerated)
Second step: Citrate further oxidized releasing 2 CO2 molecules and making 2 NADH molecules
Third step: OAA regenerated so cycle can continue - In doing so NADH, FADH2, and GTP is made
General description of Electron Transport Chain
- High energy electron carriers (NADH/FADH2) are oxidized by chain of proteins on inner membrane of mitochondria
- Energy produced doing this is used to pump protons out of matrix and lastly reduce O2 to H2O
- Proton gradient is used by ATP synthase, letting protons diffuse down gradient, powering ATP generation
Proteins on the Electric Transport Chain
1- NADH dehydrogenase (A) 2 - Ubiquinone, (Q), or CoenzymeQ 3 - Cytochrome C reductase (B) 4 - Cytochrome C 5 - Cytochrome C oxidase (C)
A, B, & C are the only ones that pump protons
How many protons pumped per NADH or FADH2?
~10 protons per NADH & ~6 per FADH2