O2-binding curves 1 0.9 0.8 2 0.7 3 0.6 0.5 0.4 0.3 0.2 0.1 100 120 20 40 60 80 po2 (torr) Fractional Saturation 4. Is curve #3 shifted more towards R- or T- state, relative to curve #2? The binding curve for oxygen is choose your answer... V for hemoglobin and for myoglobin choose your answer... V

2. The diagram to the right shows the change in the structure of the C-terminal portion of each of the ẞ-subu- nits of human hemoglobin (HbA) in the oxyHb to deox- yHb or R-to-T transition. The hydrogen bonding interac- tion of the C-terminal ẞHis 146 residue with the side chain of Asp94, highlighted by the red ellipse, has been shown to be responsible for a major portion of the proton uptake associated with the Bohr effect. Treatment of HbA with the enzyme carboxypeptidase A (CPA) results in loss of the C-terminal ẞHis 146 and ẞTyr145 residues of the ẞ- subunits. (a) ( ) Draw a Hill plot [log(Y/[1-Y]) vs. log(pO2), Y = fraction of heme groups occupied by O2] to compare the values of the Hill coefficient nн and the O2-binding affinity at pH 7.4 of normal HbA before and after treat- ment of with CPA. (b) (' ) How will the plot for CPA-digested HbA change at pH 7.2? (c) 1 Hi5146 HN- ✓ Low PK B-chain. CH2 CH-NH-CO-CH-NH- CH₂ Tyr145 он HbO2 or R state Туг145 CH-CH2- OH co NH CH CH₂ His…

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1. All oxygen inhaled by animals and transported around their bodies is destined for specific locations in the body. Once oxygen reaches protein complex IV of the electron transport chain (ETC) it begins its vital task of pulling electrons away from protein complex IV. In short, a set of chain reactions are triggered at protein complex IV. From here 2 electrons are taken from complex III, which then takes two electrons from complex II, or l. a) Use a diagram and your own words to describe how a proton-motive force created by the ETC generates ATP. Make sure you label your diagram correctly and include; inner mitochondrial membrane, hydrogen ions, ADP, P, intermembrane space, ATP synthase, mitochondrial matrix, and ATP.