The induced-fit hypothesis and the lock-and-key hypothesis are used to describe the mode of action of enzymes. Radish plants contain the enzyme peroxidase that catalyses the breakdown of hydrogen peroxide. Students investigated the effect of increasing the concentration of hydrogen peroxide on the activity of peroxidase extracted from radish. The results of their investigation are shown in Fig. 4.1. [Figure 4.1]
- (a)Explain the induced-fit hypothesis.[3]
- (b)(i)Explain the effect of increasing the concentration of hydrogen peroxide on the initial rate of reaction as shown in Fig. 4.1.[3]
- (b)(ii)The students determined the K_m for radish peroxidase as 0.10mmoldm⁻³. With reference to Fig. 4.1, describe how they determined the K_m.[2]
- (c)A further investigation found that the K_m for carbonic anhydrase is 12mmoldm⁻³. Describe the role of carbonic anhydrase in the transport of carbon dioxide.[3]
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Mark scheme
Marking points from the official mark scheme (May/June 2021). The mark or mark type is shown in brackets.
- [3] idea of shape needs to be in the answer for mp2 and mp4 \ 'substrate changes shape'
- any three from
- 1 active site is not (fully) complementary to substrate ;
- 2 active site, changes shape / moulds around, to fit the substrate ;
- A conformational change for shape change
- 3 enzyme-substrate complex / ESC, forms ;
- 4 active site returns to original shape on release of product ;
- 5 AVP;
- e.g. change of shape (to give complementary fit) lowers activation energy / puts strain on bonds / AW
- ref. to binding site / catalytic site (of active site)
- [3] A peroxidase for enzyme
- any three from
- rate of reaction increases as substrate concentration increases to 0.33 – 0.35 mmol dm⁻³
- 1 (up to 0.33 to 0.35 mmol dm⁻³) some active sites are not occupied ;
- 2 more collisions between, enzyme / active site, and substrate molecules ;
- A more collisions lead to increase in formation of enzyme-substrate complexes
- rate of reaction remains constant above 0.33-0.35 mmol dm⁻³
- 3 all active sites, occupied / saturated ;
- 4 correct reference to limiting factor for slope ; A limits / limiting
- e.g. at low substrate concentrations, substrate concentration limiting / enzyme concentration not limiting
- 5 correct reference to limiting factor for plateau ; A limits / limiting
- e.g. at high substrate concentrations, enzyme concentration limiting / substrate concentration not limiting
- [2] idea that determined Vmax / maximum rate / ref. to 5.6 (µmol min⁻¹) ;
- A if Vmax shown on graph
- Km is the substrate concentration at half the Vmax ;
- [3] any three from
- in respiring tissue
- 1 (carbonic anhydrase) catalyses the reaction between water and carbon dioxide in, red (blood) cells / erythrocytes ;
- 2 to form carbonic acid, which dissociates to form HCO₃¯ and H⁺ ;
- A from equation A use of word ion(s)
- 3 HCO₃¯, moves / passes / diffuses (through membrane proteins from red blood cells) into plasma ;
- 4 (activity of enzyme) maintains (steep) concentration gradient for diffusion of carbon dioxide into red blood cells ;
- 5 idea that so helps to remove large quantities of carbon dioxide ;
- in lungs
- 6 (carbonic anhydrase) converts HCO₃⁻ back into carbon dioxide so can be, excreted / removed / exhaled ;
- if described earlier A catalyses reverse reaction so carbon dioxide can be, excreted / AW
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