Biological processes Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

what is respiration

A
  • conversion of cehmcial energy in molecular bonds into usable energy needed to drive processes of living cells
  • respiration refers to use of oxygen, intake from environment and transport in blood

*external respiration = enterance of air into lungs and the gas exchange between alveoli and blood

*internal respiration = exchange of gas between blood and cells and intracellular processes of respiration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what are the favoured feuld sources

A

carbohydrates and fats

  • C-H bond is energy rich (Co2 has very little usable energy, its a stbale energy exhausted end product of respiration)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what id dehydrogenation

A
  • occurs during respiration, high energy hydrogen atoms are removed from organic molecules

(oxidation rxn)

  • H is accepted by an H acceptr (oxygen in final step fo ETC), this is reduction comp of redox rxn

*this oringial oxidation reuqires energy input but has net energy production forming ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what are the two main stages of glucose catabolism

A
  • glycolysis and cellular respiration
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what is glycolysis

A
  • first stage of glucose catabolism
  • involves 9 steps, in step 4 6 carbon mol is split into a 3 carbon molecule which is isomerized into PGAL (glyceraldehyde 3 phosphate)
  • one mol of glucose turns into 2 mol fo pyruvate, 2 mol of ATP and 2 mol of NADH

* production of ATP refered to as substrate level phosphorylation bc no participation of intermediate molecule like NAD+, tis directly coupled to glucose degredation

  • all occurs in cytoplasm

net reaction: Glucose + 2 ADP + 2 Pi + 2 NAD+ –> 2 Pyruvate + 2 ATP + 2 NADP + 2H+ + 2 H2O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

what happens to the pyruvate product of glycolysis

A
  • pyruvate still has most of the energy from initial glucose mol
  • if under anerobic conditions pyruvate is reduced by fermentation
  • uner aerobic conditions its further oxidized during cellular respiration in mitochondria
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

explain the process of fermentation

A
  • NAD+ must be regenerated for glycolysis to continue in absence of O2
  • pyruvate is reduced into ethanol or lactic acid, produces only two ATP per glucose moleculse

* not making any more ATP just using pyruvate to regenerate your NAD+ so glycolysis can cont

Alcohol Fermentation: occurs only in yeast and some bacteria, pyruvate produced in glycolysis is converted to ethanol to regenerate NAD+

Lactic acid fermentation: occurs in certain fungi, bacteria and human muscle during strenuous activity. When oxygen supply to muscles is not sufficient, still regen NAD+ to be used in step 5 of glycolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what is cellular respiration: the net result and the different stages

A
  • most efficient catabolic pathway to get energy from glucose
  • yeilds 36-38 ATP
  • aerobic process in which oxygen acts as the final acceptor of electrols passed along ETC
  • 3 stages: pyruvate decarboxylation, the citric acid cycle and the electron transport chain
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

explain pyruvate decarboxylation

A
  • pyruvate formed during glycolysis is transported from the cytoplasm into mitochondria matrix where is it decarboxylated
  • acetyl group is transfered to coenzyme A forming acetyl-CoA which then can enter the kerbs cycle
  • 2NAD+ is reduced to 2NADH and also 2 CO2 is released
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

explain the citric acid cycle

A
  • aka krebs cycle
  • begins w/ two carbon acetyl CoA mol which combine with oxalate ( a 4 carbon mol) to form a 6 carbon mol cirtrate
  • through the cycle two CO2 are released and oxaloacetate is regenerated

net rxn: 2 acetyl CoA + 6 NAD+ + 2FAD + 2 GDP + 2 Pi + 4 H2O —-> 4 CO2 + 6NADH + 2FADH2 + 2 GTP + 4H+ + 2CoA

-

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

explain the electron transport chain

A
  • carrier mechanism located on inside of inner mitochondrial membrane
  • during oxidative phosphorylation ATP is produced when high energy potential electrons are transferred from NADH and FADH2 to oxygen be series of carreir mol on IMM
  • as e- transfered from barrier to carrier free energy si released and used to form ATP

*most mol on ETC are cytochromes that resemble hemoglobin in the structure of their active site

*contain central iron capable of redox

  • each carreir is reducaed as it accepts an electron and then is oxidized when it passes it to the next carrier
  • last carrier is O2 which picks up a pair of hydrogen ions from surrounding medium to form

**NADH produced 3 ATP and FADH2 produces 2 ATP in ETC

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what is substrate level phosphorylation

A
  • degradation of one glucose molecule yield a net of two ATP from gylcolysis and one ATP for each turn of the citric acid cycle

*total 4 atp produced by substrate level phosphorylation

(not using NAD or FAD)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what is the production fo ATP from oxidative phosphorylation

A
  • produces more than 90% of ATP used by cells in our body
  • at the end of the ETC, respiratory enzyme pump H ions from matrix of mitochondria to intermembrane space creating a alrge conc gradient
  • H ions pass through chnnels in respiratroy enzymes along concentration gradient, energy created used to convert ADP into ATP

* two pyruvate decarboxylations = 2 NADH

*each turn of kerbs produces 3 NADH and 1 FADH2, since happens twice per glucose mol 6 NADH and 2 FADH2

  • each FADH2 generates 2 atp and each NADH generates 3 ATP
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

what are the alternative energy sources

A
  • carbohydrates, fats then proteins
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

how are carbohydrates used for energy

A
  • disaccharides are hydrolyzed into monosaccharides which can then be converted into glucose or glycolytic intermediates
  • glycogen stored in liver can be converted when needed into a glycolytic intermediate
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

how are fats used as energy

A
  • stored in adipose tissue in the form of triglycerides
  • when needed hydrolyzed by lipases to fatty acids and glycerol and carried by blood to other tissues for oxidation
  • glycerol can be concerted to PGAL (glycolytic intermediate)
  • fatty acids must first be activated in the cytoplasm, process reuqires two ATP then transported to mitochondrion and undergoes beta oxidation into 2 carbon fragments
  • fragments then converted to acetyl CoA which enters the citric acid cycle

* for each round B oxidation of a saturated fatty acid one NADH and 1 FADH2 produced

17
Q

how are proteins used as energy

A
  • amino acids undergo transamination reaction: lose an amino group to form a alpha-keto acid
  • carbon atoms of most amino acids are converted into acetyl CoA, pyruvate or an intermediate of the citric acid cycle
18
Q

what is oxidative deamination

A
  • removes an ammonia molecule direcctly from the aminoa cid
  • amminoa is toxic in certebrates
19
Q

what are enzymes

A
  • organic catalysis: affect rate of reaction w/o itsel fbeing changed
  • decrease activation energy
  • proteins, somtimes conjugated and have a nonprotein coenzyme (both must be present for enzyme to function)
  • highly seletive
  • do NOT alter equilibrium constant
  • are NOT consumed in reaction
  • are pH and temp senstive
20
Q

what is the lock and key theory

A
  • spatial structure of an enzymes active site is exactly complementary to spatial strucutre of its substrate
21
Q

what is enduced fit theory

A
  • active site has flexibilty of shapre
  • when approprate substrate comes in contact w/ active site the conformation of active site changes to fit the substrate
22
Q

enzyme specificity

A
  • enzyme action is dependent on temp, pH and conc of enzyme and substrate
  • as temp inc rte of enzyme inc intil optimal temp is reached: beyond that the shape of active site is altered and deactivates enzyme
  • opperate at an optimal pH, typically 7.2, unless something like pepsin which works in stomach at pH2
  • inc of conc of substrate inc rate until all active sites of enzyme is occupied, then reach a Vmax where inc substrate conc will not help
23
Q

explain competitive inhibition

A
  • active site is specfici for particular substrate or class of substrates, similar mol can bind
  • is conc are similar will be competition of occupation fo active site
  • can outcompete if inc the concentration of substrate
24
Q

explain noncompetitive inhibition

A
  • inhibitor forms a strong covalent bond w/ enzyme making ti unable to bind with tis substrate
  • noncompetitor cant be displaced (irriversible inhibition)
  • excess substrate will not help, rxn will never reach Vmax
  • can have allosteric inhibition in which inhibitor binds to another site than active but it changes the shape of the active site
25
Q

what is hydrolysis

A
  • reaction functions to digest large molecules into smaller components
    ex: lactases hydrolyze lactose into monosaccharides glucose and galactose
26
Q

what do proteases and lipases

A
  • proteases degrade proteins into amino acids
  • lipases breaj down lipids into fatty acids and glycerol
27
Q

what are cofactors

A

non protein molecule, required by a lot of enzymes to become active

  • can be metal cations like ZN2+ and Fe2+ ot small organic groups called coenzymes
  • most coenzymes cannot be synthesized in the body and must be obtained from diet as vitamin detivates
  • cofactors bind to enzyme by strong covalent bonds called prosthetic groups