Biological Oxidation Flashcards
- Final stage of cellular respiration?
- ETC occurs in?
- How many protein complexes? And uses what?
- How It generates ATP?
- Summarize ETC?
- ETC
- Inner mitochondrial membrane
- Complex I —-
Complex II
Complex III
Complex IV
Complex I —- uses NADH
Complex II — uses FADH2
- By utilizing the energy stored in proton gradient
- The Electron Transport Chain (ETC) is the final stage of cellular respiration, occurring in the inner mitochondrial membrane. It involves a series of protein complexes that transfer electrons from NADH and FADH₂ to oxygen, creating water. As electrons move through the chain, protons are pumped across the membrane, generating a proton gradient. This gradient drives ATP synthase to produce ATP, the main energy currency of the cell. The ETC is essential for efficient energy production in aerobic organisms.
- Conditions for ETC?
- Final electron acceptor?
- Where does ETC, Glycolysis and kreb cycle occur?
- What are F1 particles?
- Which complex is responsible for ATP synthesis?
- Of. NADPH & NADH which one is used for ETC?
- Aerobic (O2 needed)
- O2 (to generate H20)
-
Electron Transport Chain (ETC): Occurs in the inner mitochondrial membrane.
- Glycolysis: Takes place in the cytoplasm of the cell.
- Krebs Cycle (Citric Acid Cycle): Occurs in the mitochondrial matrix.
-
Electron Transport Chain (ETC): Occurs in the inner mitochondrial membrane.
- Knob-like structures on inner surface of inner mitochondrial membrane
- phosphorylating subunits
Centres for ATP production - Complex V
- NADH —– For ETC
NADPH —– For Anabolic erxn (e.g fatty acid synthesis, cholesterol synthesis)
- What is a flavoprotein?
Give examples? - Succinate dehydrogenase converts succinate to?
- Coenzyme Q is also known as?
- It has which side chain?
- What is CoQ10?
- Coenzyme Q can accept electrons from?
- Precursor of coenzyme Q?
- Which organisms donot have coenzyme Q?
- A flavoprotein is a type of protein that contains a flavin molecule, such as flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD), as a prosthetic group. These flavin molecules are important for various biological processes, including oxidation-reduction reactions, where they help transfer electrons.
E.g
NADH dehydrogenase (coenzyme FMN )
Succinate dehydrogenase
(Coenzyme FAD)
- Fumarate
- Ubiquinone
- Isoprenoid side chain
- Mammalian tissue has a quinone with 10 isoprenoid units which is known as coenzyme Q10
- Both Complex I & II
NADH dehydrogenase (NADH)
Succinate dehydrogenase (FADH2) - None – directly synthesized in body
-
Mycobacterium
Vitamin K performs function of CoQ
- What is cytochrome Oxidase?
- Only electron carrier the heme of which reacts with O2?
- Molecular weight of Cytochrome C?
How many amino acids? - The order of electrons transport from CoQ to cytochrome?
- What are cytochrome? Their structure?
How does it differ from that of Hb? - Name inherited disorders of ETC?
- Cytochrome a and cytochrome a3 are collectively called cytochrome oxidase
- Cytochrome oxidase
- 13,000
—104 - CoQ– b—c1— c —- a—- a3
- Congugated proteins containing heme group
— porphyrin.ring with iron at centre
– but unlike Hb (where iron is ferrous Fe+2), the iron in cytochrome is alternatively oxidized and reduced (Fe+3 —- Fe+2) - (MELAS)
Mitochondrial Encephalopathy
Lactic Acidosis
Stroke
- MELAS are inherited disorders due to deficiency of?
Caused by? - MELAS are belived to be involved in which diseases?
- Fatal Infantile Mitochondrial Myopathy is caused by reduced or absensce?
- Complex I (NADH–Q oxidoreductase)
Complex IV ( cytochrome oxidase)
- mutations in mitochondrial DNA
- Alzheimers
Diabetes mellitus - Oxidoreductases of ETC
- How many ATPs produced for (P:O);
NADH
FADH2 - Name the sites for oxidative phosphorylation in ETC?
- Coupling sites for;
NADH
FADH2
And how many protons? - Each ATP gives how many cal of energy?
- Give percentage of energy given by NADH oxidation?
- NADH —— 2.5 (P:O = 2.5)
FADH2 —— 1.5 (P:O = 1.5) - • oxidation of FMNH2 by CoQ
• oxidation of cytochrome b by cytochrome c1
• cytochrome oxidase rxn - NADH —— 3 (Proton = 10)
FADH2 —— 2 (proton = 6)
As the first site is by passed - 7.3 Cal
- 35% in form of 2.5 ATP
- How chemical coupling hypothesis and chemiosmotic hypothesis differ?
- What are the functional subunits of ATP synthase?
- Composition of F0 subcomplex?
- Structure of F1 ATPsynthase?
- Proton influx rotates which subunit? And confirmational change in which leads to Atp synthesis?
- Confirmations of B subunits?
- Chemical coupling—- phosphorylated high-energy intermediates produced which synthesize ATP
Chemiosmotic—– proton gradient created which is used by ATP Synthase for ATP
- F1 & F0
- Composed of channel protein-C to which F1-ATP synthase is attached
-
Central y-subunit
Surrounded by alternating 3 alpha & 3 beta subunits - Rotation—- y-subunit
Confirmational change — B3 subunits -
Open (O) (ATP release)
Loose (L) (ATP & Pi binds)
Tight (T) (ATP synthesis)
- Worlds smallest molecular motor?
- Inherited disorders oF ETC or oxidative phosphorylation are inherited from?
- Out of mitochondrial DNA and mitochondrial, which one is more susceptible to mutation??
- How many polypeptides are required for oxidative phosphorylation? And coded by?
- What is laber’s heriditary optic neuropathy?
- Pearson and leigh syndrome?
- Atp synthase
- Mother to child
(Because mitochondrial DNA is inherited by mother, bcz sperm can’t pass on mit.DNA to fertilized ovum) - Mitochondrial DNA —-ten times more susceptible
4.100
13 coded by —- mit. DNA
(& Synthesized in mitochondria)
Rest in nuclear DNA
(In cytoplasm)
- An inherited disorder of oxidative phosphorylation
- mutation in mit.DNA
- loss of bilateral vision
- neuroretinal degeneration - Both are inherited disorder of oxidative phosphorylation;
- Leigh Syndrome: A severe neurological disorder causing developmental delays and muscle weakness, often starting in early childhood.
- Pearson Syndrome: A rare condition affecting the bone marrow and pancreas, leading to anemia and other health issues, typically beginning in infancy.
- Inhibitors of complex
I, II, III, IV? - most potent inhibitor of ETC?
Leads to death due to? - Treatment of Cyanide poisoning?by which antidotes? How do they work?
-
Complex I:
Rotenone (fish poison)
Amytal (barbituate drug)
Piercidin A (antibiotic) -
Complex II:
Malonate -
Complex III:
Antimycin A
British Antilewisite (BAL) (war-gas antidote) -
Complex IV:
Cyanide,
Carbon Monoxide
Hydrogen sulphide
Azide
(CO —- react with reduced form of cytochrom
While
Cyanide & Azide —- with oxidized
-
Complex V:
Oligomycin
- Cyanide poisoning
—tissue asphyxia - Antidotes
•Amyl Nitrate
•Sodium Nitrite
- convert hb to meth.Hb that binds to Cyanide —- cyanomethemoglobin— release cyanide from cytochrome
•Hydroxycobalamine (a form of vitamin B12)
- converts cyanide to harmless cyanocobalamine
- What are uncouplers?
- Give names of uncouplers?
- Physiological uncouplers?
- Side effect of 2,4-DNP?
5.. what are ionophores?
Name ionophores for K+ ion?
- What is Atractyloside? It’s effect on oxidative phosphorylation?
- That uncouple (unlink) ETC from oxidative phosphorylation
- disrupt proton gradient
- increase membrane permeability to H+ (so move back to matrix without Atp synthase)
- produce heat but No ATP - •2,4 Dinitrophenol (DNP)
• Dinitrocresol
• Pentachlorophenol
• TrifluoroCarconylCyanidePhenylhydrazone (FCCP)
• Aspirin
• Thermogenin
• Thyroxine
• Long chain free fatty acids - Thyroxine
Thermogenin (UCP1) - Hyperthermia
- Lipophilic substances
- transport of ion across membrane
For K+;
• Valinomycin
• Gramicidin A
• Nigercin
- A plant toxin
- inhibits adenine Nucleotide Carrier (that carries ADP & ATP)
-blocks adequate supply of ADP
So no phosphorylation
- Categorize the enzymes of biological oxidation?
- Name oxygenases? Categorize?
- Examples of hydrogen peroxidases?
- Name oxidases?
- Name the oxidase that results in production of H2O2 Instead of H20?
- Name dehydrogenase?
- These are oxidoreductases;
• Oxidases (removes H2 and adds to an O2 proton acceptor)
•Dehydrogenases (removes H2 but no O2 acceptor)
•Hydroperoxidases
•Oxygenases (adds O2 directly)
2 . 2 Categories;
Dioxygenases (true) (adds both O-atom)
E.g;
Homogentisate oxidase
L-tryptophan pyrrolase
Monooxygenases (mixed function)
(Only 1 O- atom added)
E.g;
Cytochrome P450 monoxygenase system of microsomes
- Peroxidase
Catalase - E .g,
Cytochrome oxidase
Tyrosinase
Monoamine oxidase (H2O2 formed instead of H20)
Some flavoproteins;
L-amino acid oxidase (FMN)
Xanthine oxidase (FAD)
- Monoamine oxidase
- All the cytochromes (b, c1,c) except cytochrome oxidase
- What are shuttle pathways? Name them?
- Reducing equivalents used by each?
And ATP produced? - Malate- asparatate shuttle occurz in?
Creatinine phosphate occur in? - Conversions in malate-aspartate & glycerol-phoshaate shuttle?
- Oxaloacetate in mitochondria undergoes transamination with glutamate to give?
- In creatinine phosphate shuttle, phosphate moves from??
7.. give cytosolic and mitochondrial isoenzymes of creatine kinase?
- Transport electrons produced in cytosol from NADH —– to mitochondria
• Glycerol-Phosphate Shuttle
• Malate-Aspartate shuttle
• Creatinine phosphate shuttle - • Glycerol-Phosphate Shuttle —- FADH2 —- 1.5 ATP
• Malate-Aspartate shuttle —- NADH —- 2.5 ATP - Malate-Aspartate —-
liver
Heart
Creatinine-phosphate
Skeletal muscle
Heart
4.
• Glycerol-Phosphate Shuttle
Dihydroacetone phosphate (in cytosol) —– Glycerol-3-Phosphate (move into mitochondria)
• Malate-Aspartate shuttle
Oxaloacetate (in cytosol) —– Malate (move into mitochondria)
- Aspartate
a-ketoglutarate - Mitochondria —- cytosol (opposite to other to shuttles)
-
Cytosolic
BB
MB
MM
Mitochondrial
Ubiquitous
Sarcomeric