can x ray or mass spec detect a metal ion bound to a protein
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A coworker has just isolated a copper enzyme that catalyzes the conversion of oil sludge into soluble alcohols in the presence of O2. There are two Cu atoms per protein, which consists of a single polypeptide chain. As the bioinorganic chemist on the project, you are given unlimited quantities of the protein for the purpose of determining the active site structure. You have at your disposal a number of physical techniques, including NMR and EPR spectrometers, a magnetic susceptometer, a Mössbauer instrument, an X-ray absorption beamline, a UV-Vis spectrophotometer, a Raman/IR spectrometer, but alas, no X-ray diffractometer. You have time to complete measurements by only three techniques before you have to give a report to your colleague. Describe what measurements you would make and in what order you would make them to get the most out of your time, what results you might expect, and how you would use this information to characterize structurally the dicopper center. Include in your discussion the kinds of ligands that you would be looking to identify and how the methods might allow you to make such a determination.
Sri K.
Suppose that an EXAFS experiment shows the presence of peaks at 2.1 and 2.3 Å for a protein with a metal cluster. What is the best interpretation? a. There is a Lys residue coordinating a Fe2+. b. There is a Cys residue coordinating a Fe2+. c. The cluster has two Fe2+ metals coordinated by His residues. d. The cluster has two Fe2+ and two Mn2+ coordinated by 2 Cys and 2 His residues.
Madhur L.
Lab work is lost and you no longer know what color two created complexes should be. (Fe(III) and [Cu(diaminobutane)3]+) What other properties can be used to tell them apart? List the theory, instruments, and results you can use to identify them without spectrophotometry: (I think one of them can be magnetism? you can ignore the example complexes, I just want to know what theories would help explain them. Should it be crystal field theory lab?)
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