The structure of a metalloenzyme active site is down below(black picture). Describe, from a chemical and structural perspective, how the reactive site is designed to facilitate its catalytic reaction. The example below(white pitcure) suggests the level of detail that is required. Make sure that you explain what the metal is doing, what the reaction is, and its biological significance.
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The structure of a metalloenzyme active site is down below(black picture). Describe, from a chemical and structural perspective, how the reactive site is designed to facilitate its catalytic reaction. The example below(white pitcure) suggests the level of detail that is required. Make sure that you explain what the metal is doing, what the reaction is, and its biological significance.
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- Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.Describe the metabolic lifestyle for each of the following organisms. Your description should address where/how each organism (i) acquires energy (ATP &NH3 i, CH₂ HN 'S Co A NH CH₂ CH₂ NH 1. Describe the role of Cys in the catalytic mechanism shown. 2. Describe/predict the microenvironment that could allow for Cys to be ionized in the catalytic mechanism.
- Energy conservation in microorganisms can be highly diverse. Technically, any pair of electron donor (donates electrons and is oxidized) and electron acceptor (accepts electrons and is reduced) that forms a redox reaction with positive reduction potential can support microbial growth, although many of them have not been observed. Calculate how many moles of ATP can theoretically be generated from 1 mole of sulfur (So/SO4-) as the electron donor and nitrate as the electron acceptor (NO3-/N2).On the right the Hill plot com- (b) pares the O2 binding properties of Hb Ya- kima with those of HbA in 0.1 M NaCl buff- Hb-Yakima ered to pH 7 with 0.01 M bis-Tris. Focus first on the line for "stripped Hb". This is the term for hemoglobin isolated from erythro- cytes with removal of all organic phosphate molecules that might bind to the protein in RBCS. You can see that 2,3-bisphospho- glycerate (BPG; labeled DPG according to old terminology) does not alter the O2 bind- ing affinity of Hb Yakima in contrast to HbA (although it was shown that BPG did bind to the deoxyHb Yakima molecule). Also, Hb Yakima is associated with markedly decreased allostery in the absence and presence of BPG, in comparison to HbA. IHP = inositol hexaphosphate, an artificial allosteric modifying ligand that binds more tightly than BPG. stripped Hb Hb-A •DPG +DPG n= 1.0 n = 2.3 n=2,5 +THP +IHP 0.5 0.5 1 5 10 50 po, ( mm Hg ) %3D On the right is a diagram copied from the lecture handout "Hemoglobin and Allo-…Although physiologically distinct, aerobic chemolithotrophsand chemoorganotrophs share a number of features withrespect to the production of ATP. Discuss these commonfeatures along with reasons why the growth yield (gramsof cells per mole of substrate consumed) of achemoorganotroph respiring glucose is so much higherthan for a chemolithotroph respiring sulfur
- In carbonic anhydrase II, mutation of the proton-shuttle residue His 64 to Ala was expected to result in a decrease in the maximal catalytic rate. However, in buffers such as imidazole with relatively small molecular components, no rate reduction was observed. In buffers with larger molecular components, significant rate reductions were observed. Propose an explanation.Certain bacteria can respire in anoxic environments using arsenic (V) as electron acceptor. The relevant unbalance half reactions are: H₂ AsO+H → H¸AsO +H₂O, logK = 10.84, AG = -14.5kca I m I ol-e CH₂O+H₂OH + CO2 (g), logK = 1.2, AG° = -1.63kca — ol-e 1) Balance the two half reactions 2) What is m the overall respiration reaction, standard free energy change \Delta GO 3) Is this process energetically more or less favorable than sulfate reduction? (\Delta GO for the reduction of sulfate to HS- is -5.78 kcal/mol - e-) 4) If [H2AsO4-] = [ H3ASO3] = 0.5 mM and pH = 7, estimate pe of the systematric acid Citric Acid Cycle Notes? atrate Step 1: fynthalt) H-C-COOH M-C-C00⁰ Step 3: Step 5: H-O-C-COOH D-C-Cooe 1 H-C-COOH -C-COO Step 7: H- CH₂-C-GA ( H Citric Acid K A) Which steps require NAD+? B) Which steps require FAD? Comu. base of Citric and (isocitrate) 4 Step 2.--COM 1 И-С-СООН по-с-соон 2 alcohol H Step 4: Step 6: Step 8: ан, котодвинов 4-Ć-COOH нс-н OT 1-C-COOH to gluctasote decarboxylation 2. keto g (Reduced Coenzymes] Cycle - NAPH/H+ FADH₂
- several days. 20. The apparatus below were used to investigate whether yeast in glucose solution produce carbon(IV) oxide in the absence of oxygen. (a) Ide rep (i) (ii) (b) Sta pat 22. The up rele Oil film flas Lime water dur yeast + 10% Glucose solution (a) Explain how you could remove dissolved oxygen from the 10% glucose solution before the experiment commences. (b) State what would happen to the lime water as the experiment proceeds to the end. (c) Explain what would happen if the temperature of glucose solution with yeast raised from room temperature to 37°C. Flask A a)Give oil b) Stat this ezuation The mrocess represented.10 glucose molecules are used in anaerobic respiration. How many ATP will be yielded under these conditions?1) Biochemists use and define a standard transformed Free Energy (ΔG’o), what is all this notation stuff about anyway? 2) What is the mathematical relationship between ΔG’º and K’eq ? 3) What is the single biggest driver of the observed Keq ?