The order in which the various conveying bodies are arranged in the respiratory chain.

(i) The value of the standard redox bit indicates the size of the redox capacity, the greater the negative value of the standard redox bit, the stronger its reduced properties, easy to be oxidized; Therefore, the order of the various parts in the respiratory chain should be arranged from low to high in turn (Figure -4).

Figure 6-4 standard redoxionity of various conveyor

2. According to the oxygen conditions when the oxidation reaction reaches equilibrium, the reduction degree of the various conveyor is determined. Chance and Williams used phosphorescies to determine the degree to which the various transfer bodies in the respiratory chain were reduced when the off-body mitochondrials reached equilibrium in the cycle of triamlic acid under aerobic conditions. When the reaction reaches equilibrium, the reduction of the various conveying bodies from one side of the substrate to the oxygen side shall be decreasing, with the highest on one side of the substrate and the lowest on the oxygen side, as shown in the data in the table below.

table 6-1 aerobic dynamic balance when the electron conveys the degree of reduction

FP: yellow protein

"tt1" > this situation is like a physical connection tube, Figure 6? A, if the incoming water is equal to the amount of water flow, that is, when the flow reaches equilibrium, the water level in the nearest water pipe from the incoming water intake is the highest, the water level in the water pipe closest to the water pipe is the lowest, the water level from the incoming pipe to the water pipe is gradually reduced, if the water flow is regarded as an electronic flow, this is the case in the above experiment.

3. The use of specific inhibitors specific inhibitors can block specific links in the respiratory chain, blocking the site of the substrate side of the various conveyors should also prototype, blocking the site of oxygen one The various transfer bodies on the side should be oxidizing type, just as we block the bottom of the Unicom pipe, the water in the previous pipes in the blocking site is full, and the water in the water pipes after the blocking site is flowing light (see Figure 6-5, B).

Figure 6-5 oxygen oxidation stability when the reduction of various conveyants is too fraction

A. without inhibitor B. Add anti-mold A blocking

complex I.: catalytic NADH oxidation, CoQ reduction.

complex II.: catalytic acid oxidation, CoQ reduction

complex III.: Catalytic Co QH2 oxidation, Cyt c reduction

complex IV.: Catalytic Cyt c oxidation, O2

from the table can be seen that FP, Cyt b is located in the antimycin A blocking site before Cyt c, cl, aa3 is after the blocking site. By using different inhibitors for this experiment, the order of the various conveyors in the respiratory chain can be determined.

4. In in-body experiments, mitochondrials are divided into complexes, their respective catalytic reactions are detected, and then recombined to test their catalytic capacity.

with the above experimental method, the order of the components of the respiratory chain has been basically clear, but there are still some inconsistent views, including CoQ to cytochrome C part of the study is not clear, Fe-S and CoQ positioning and quantity is also controversial.

(ii) oxidized respiratory chain

"tt1" >1.NADH oxidized respiratory chain most peopledehydrogenase are used as coenzymes by NAD plus, hydrogen taken off in dehydrogenase catalytic substrate SH2 is handed over to NAD plus to generate NADH plus H, and under the action of NADH dehydrogenase, NADH plus H. Two hydrogen atoms are passed to FMN to generate FMNH2, and then hydrogen is transmitted to CoQ to generate CoQH2, at which point the two hydrogen atoms are dissofided into 2H plus 2e, 2H plus free from the medium, and 2e is released into the medium. Cyt b, c1, c, aa3 pass, and finally pass 2e to 1/2O2, generating O2-, O2 and the media free 2H plus combined to generate water, combined with the above transfer process can be represented by Figure 6-6.

Figure 6-6 NADH oxidation respiratory chain

SH2: actum; (Fe-S): iron sulfur center; Cyt: cell pigment

. Amber acid oxidation respiratory chain Amber acid dehydrogenation under the action of amber acid dehydrogenase to produce Yanhuso acid, FAD accepts two hydrogen atoms to generate FADH2, and then transfer hydrogen to CoQ to produce CoQH2, after which the transmission and NADH oxidation respiratory chain is the same, the entire transfer process can be represented by Figure 6-7.

Figure 6-7 amber acid oxidation respiratory chain

(Fe-S): Iron Sulphur Center: b: serotonin of the amber acid dehydrogenase complex

3. Mitochondrial oxidation respiratory chain Summary The metabolism of substances in mitochondrials produces a large number of NADH-H-plus and FADH2-they can come from acetone oxidation dehydration, triacetonic acid circulation, fatty acids β-oxidation and L-glutamate oxidation de-ammonia and other reactions, and now some important substrate oxidation of the respiratory chain summarized in Figure 6-8.

Figure 6-8 respiratory chain when certain substrates oxidize

ETF: Electronic delivery of xantin protein, supplemented by FAD