Biochemistry

You might also like

Download as pdf or txt
Download as pdf or txt
You are on page 1of 4

Biochemistry assignment 3

Name :- Rahaf Fathallah Murshed

Studant NO. :- 202111999

Q1: compare between competitive inhibition and noncompetitive inhibition from: (3 mark)

- Function

- Effect on Vmax

- Effect on Km

Competitive inhibition :-
occurs when the inhibitor binds reversibly to the same site that the substrate would normally occupy
and, therefore , competes with the substrate for that site.

1. Effect on Vmax: The effect of a competitive inhibitor is reversed by increasing [S].

2. Effect on Km: A competitive inhibitor increases the apparent Km for a given substrate. This
means that, in the presence of a competitive inhibitor, more substrate is needed to achieve
1⁄2Vmax.

Noncompetitive inhibition :-
● Noncompetitive inhibition occurs when the inhibitor and substrate bind at different sites on the
enzyme. ● The noncompetitive inhibitor can bind either free enzyme or the enzymesubstrate
complex, thereby preventing the reaction from occurring.

1. Effect on Vmax: Noncompetitive inhibition cannot be overcome by increasing the


concentration of substrate . ● There fore , noncompetitive inhibitors decrease the apparent Vmax
of the reaction.

2. Effect on Km: Noncompetitive inhibitors do not interfere with the binding of substrate to
enzyme. Therefore, the enzyme shows the same Km in the presence or absence of the
noncompetitive inhibitor.

Q2 In electron transport chain, discus: (4


marks)
- The mechanism of transporting electrons through :

- complex I

NADH dehydrogenase:
● The free proton plus the hydride ion carried by NADH are transferred to NADH dehydrogenase.

● Protein Complex I embedded in the inner mitochondrial membrane. Complex I has a tightly bound
molecule of flavin mononucleotide (FMN).

● a coenzyme structurally related to FAD that accepts the two hydrogen atoms (2e– + 2H+), becoming
FMNH2.

● At Complex I, electrons move from NADH to FMN to the iron of the iron-sulfur centers( in peptide
Subunits of NADH) and then to coenzyme Q.

● As electrons flow, they lose energy. This energy is used to pump protons across the inner
mitochondrial membrane, from the matrix to the intermembrane space ( important)

- complex IV.

Cytochrome a + a3:
● This cytochrome complex (Complex IV) is the only electron carrier in which the heme iron has an
available coordination site that can react directly with O2 (cytochrome oxidase).

● At Complex IV, the transported electrons, O2, and free protons are brought together, and O2 is
reduced to water

● Four electrons are required to reduce one molecule of O2 to two molecules of water.

● Cytochrome oxidase contains copper (Cu) atoms that are required for this complicated reaction to
occur.

● Electrons move from CuA to cytochrome a to cytochrome a3 (in association with CuB) to O2

‫هذا‬
‫المطلوب‬

‫هذا‬
‫المطلوب‬
- How is electron transporting chain providing the reaction of synthesis of ATP with energy .

● As electrons are passed down the ETC, they lose much of their free energy.

● This energy is used to move protons across the inner mitochondrial membrane , creating a proton
gradient that drives the production of ATP from ADP and inorganic phosphate (Pi),

● The coupling of electron transport with ATP synthesis is called oxidative phosphorylation often
denoted as OXPHOS. It proceeds continuously in all tissues that contain mitochondria .

● The remainder of the free energy not trapped as ATP is used to drive ancillary reactions such as
calcium transport into mitochondria and to generate heat.

● Q2: Incomplete reduction of oxygen to water in ETC produces reactive oxygen species (ROS),

- Write examples of these species.

such as :
1- superoxide (O2 – •),

2- hydrogen peroxide (H2O2),

3- hydroxyl radicals (OH•)

- how can the body defenses against these species.

● ROS damage DNA and proteins and cause lipid peroxidation

●Enzymes such as superoxide dismutase (SOD), catalase, and glutathione peroxidase are cellular
defenses against ROS.

Q3: ( 2 marks)
Discus the mechanism of digestion of dietary carbohydrates.

● The principal sites of dietary carbohydrate digestion are the mouth and intestinal lumen.
● This digestion is rapid and is catalyzed by enzymes known as glycoside hydrolases (glycosidases ) that
hydrolyze glycosidic bonds.
● The final products of carbohydrate digestion are the monosa –ccharides , glucose , galactose , and
fructose that are absorbed by cells of the small intestine.

You might also like