Answer Happy

PLease show all steps, not copy and paste one answr I upvote
correct steps
1. You are busily working in lab one day and discover a new dicopper enzyme, which you name hydroxymethyl carboxylase (HMC). You determine the dicopper active site binds dioxygen in one of two possible binding motifs (Figure 1). Cu cui "End on" trans-u-1,2-peroxo "Side on" u-n2:n-peroxo Figure 1: HMC binding Motifs With your adviser eagerly awaiting results, you need to figure out how to distinguish between the two configurations. Use your knowledge of point groups and molecular symmetry to determine if IR spectroscopy will allow you to identify the dioxygen binding motif of HMC (hint: consider how many vibrational features are expected for each binding motif). For simplicity, only consider the Cuz(O2) core and neglect any vibrations from the larger protein environment. (10 points) a. Identify the point group for each of the motifs. b. Determine the total degrees of freedom for each motif. Determine the reducible representation (CRR) for the total degrees of freedom for each of the motifs. d. Reduce each CRR to its irreducible representations (lir, describing all molecular motions for the molecule). Use ir to confirm the degrees of freedom of the molecule by assigning rotational, translational, and vibrational modes. f. Identify which vibrational modes are infrared (IR) active. g. Can IR spectroscopy be used to distinguish between the motifs? Why, or why not?