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- Four electron carriers, a, b, c, and d, whose reduced and oxidized forms can be distinguished spectrophotometrically, are required for respiration in a bacterial electron-transport system. In the presence of substrates and oxygen, three different inhibitors block respira- tion, yielding the patterns of oxidation states shown below. What is the order of the carriers in the chain from substrates to O2, and where do the three inhibitors act? Carriers Inhibitor a b P 1 R 2 R R R 3 R R O and R indicate fully oxidized and fully reduced, respectively.Remember the model complex by Collman et al. for the cytochrome c oxidase (CcO) active site attached to a gold electrode (see Figure). Like Cco, this complex is capable of carrying out the 4-electron reduction of dioxygen to water under constant electron flux (with the possible formation of hydrogen peroxide as an intermediate). Me HỒ HN NH NH EN- NFour electron carriers, a, b, c, and d, whose reduced and oxidized formscan be distinguished spectrophotometrically, are required for respirationin a bacterial electron transport system. In the presence of substrates andoxygen, three different inhibitors block respiration, yielding the patterns ofoxidation states shown below. What is the order of the carriers in the chainfrom substrates to O2, and where do the three inhibitors act?O and R indicate fully oxidized and fully reduced, respectively.
- The photosynthetic process used by the green sulfur bacteria, under anaerobic conditions, is best represented by which of the following balanced equations? cell bio 6CO2 + 12H2S C6H12O6 + 6S2 + 6H2O C6H12O6 + C6H12O6 C12H22O11 + H2O 6CO2 + 12H2O C6H12O6 + 6O2 + 6H2O C12H22O11 + H2O C6H12O6 + C6H12O6 C6H12O6 + 6O2 + 6H2O 6CO2 + 12H2OUse curve arrows to show the mechanism for the proposed conversion of 2a, 2b, 2c, and 2d to 4. Based on the evidence presented, which is the most likely pathway? Explain the rationale for your choice. Scheme 1 H Но HN H+ 02 + 2 H+ + 2 e- + H20 ÖH* H,O 1 2a 3 wwhm = a nucleophilic site on glutathione/cellular protein Scheme 2 HN + H,O H+ 02 + 2 H+ + NADPH +H,0 + NADP 2b 3 mhm = a nucleophilic site on glutathione/cellular protein Scheme 3 Bio. BioH BioH Bio• 20 HN X. 3 Bio• H RioH N. 4 O:The Relative Efficiency of ATP Synthesis in Noncyclic versus Cyclic Photophosphorylation If noncyclic photosynthetic electron transport leads to the translocation of 7 H+/2e- and cyclic photosynthetic electron transport leads to the translocation of 2 H+/e-, what is the relative photosynthetic efficiency of ATP synthesis (expressed as the number of photons absorbed per ATP synthesized) for noncyclic versus cyclic photophosphorylation? (Assume that the CF1CF0-ATP synthase yields 3 ATP/14 H+.)
- Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?Which of the following statements regarding the catalytic mechanism of superoxide dismutase is true? The D residue does not participate in acid-base catalysis during the course of the catalyzed reaction All of the answers are true The coordinated Zn2+ participates in stabilizing Cu²+ in the reduction-oxidation reactions to consume O₂ The Cu²+ coenzyme is coordinated by H residues, positioning it precisely for consumption of 0₂ The overall reaction consumes two equivalents of O₂ and two proton equivalents in order to produces one equivalent H₂O21 of 1 3. A sample of glucose reacts in anaerobic respiration. The right- hand box below shows a particle diagram of the moles of substances present after the reaction is complete. fe On a piece of paper draw the "Before" box as shown and draw a particle diagram of the reactant molecules that produced the mixture shown on the right. Key = C2H5OH = CO2 = CgH1206 Sub Before After You will need to draw a diagram to answer this question. On a piece of paper, draw the "Before" box as shown, and then draw a particle diagram of the reactant molecules that produced the mixture shown on the right. Upload an image of your drawing by clicking "Upload files" or by dragging and dropping your file into the box. Or, use your device's camera to take a photo of your work by clicking the camera icon.
- Put the steps of the chymotrypsin's enzymatic reaction in order of events from #1-10. -Tetrahedral intermediate collapses and product 2 released. -Aromatic R group of polypeptide substrate is positioned in hydrophobic pocket and the carbonyl of that residue is positioned in the oxyanion hole -His57 deprotonates Ser195 -Formation of acyl-enzyme intermediate -Triad in original form with Asp102 hydrogen bonding with His57 and His57 hydrogen bonding with Ser 195. -Tetrahedra intermediate collapses and product 1 released -H2O enters active site of chumotrunsir -Ser195 does nucleophilic attack on carbonyl of substrate positioned in oxyanion hole -His57 deprotonates H20 -H20 does nucleophilic attack on carbonyl of substrate in oxyanion holePropose structures for intermediates A and B in the scheme below. This three-step conversion is carried out by enzymes that require no redox cofactors (no FAD, NADH etc.) nor TPP. Which enzyme in the citric acid cycle has an activity most similar to enzyme 1? Which enzyme in the PPP or the citric acid cycle has an intermediate that bears similarity to intermediate B? H OH COO™ Enzl A Enz2 B Enz3 OHElectrons are continuously transferred from higher-energy carriers to lower-energy carriers in the electron transport chain, yet somehow iron is utilized as an electron carrier multiple times. Choose the most likely reason why this is possible. The pH of complex II is slightly higher than the pH of complex III. The reduction potential of flavin mononucleotide (FMN) in complex I is higher than the reduction potential of iron. The redox potential of iron ions can be manipulated by their environment. For instance, the iron in an iron-sulfur cluster will have a different redox potential than the iron in a heme group. The electrons carried by NADH are higher energy than the electrons carried by FADH2.