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4. 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 beam line, a UV-VIS spectrophotometer, a Raman spectrometer, a magnetic circular dichroism instrument, 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, 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.

4. 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 beam line, a UV-VIS spectrophotometer, a Raman spectrometer, a magnetic circular dichroism instrument, 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, 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.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Study problem 2 4. 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 beam line, a UV-VIS spectrophotometer, a Raman spectrometer, a magnetic circular dichroism instrument, 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, in what order you would make them to get the most out of 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. your
Transcribed Image Text:Study problem 2 4. 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 beam line, a UV-VIS spectrophotometer, a Raman spectrometer, a magnetic circular dichroism instrument, 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, in what order you would make them to get the most out of 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. your
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