User talk:Philip C. Sharpe

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Contents

Bio-inorganic Workshop

The contents of this box will change as you click on the the green links below. You can use the mouse to rotate the structure and to zoom in on sections of interest.

Drag the structure with the mouse to rotate

Read through the instructions on the accompanying worksheet. The tutorial today is about learning how to look at structures of metallo-proteins and understanding how the structure of the metal centre relates to the function of the protein.


Liver alcohol dehydrogenase, a Zn containing enzyme

The structure on the right is that of liver alcohol dehydrogenase. Clicking on any of the green links below will change the structure displayed in the box.

Urease

Click on the green link below to load the structure of urease. The structure has a pyrophosphate inhibitor bound which has only been partially displayed for the sake of clarity.

You will also need the link below to a review article in "Chemistry of Ni2+ in Urease: Sensing, Trafficking, and Catalysis" B. Zambelli, F. Musiani, S. Benini and S. Ciurli, Accounts of Chemical Research 2011, 44(7), 520-530.

[1]

Pseudoazurin

This copper-containing protein acts as an electron transfer protein.The azurin part of the name comes from the intense blue colour of this protein.

Heme proteins

In this section, we will look at 3 heme-containing proteins. The three proteins and their functions are described below. Your task is to use the information given and your knowledge of transition metal chemistry to match the structures with the correct protein. (This section of the workshop is based on the article by G.B. Ray and J.W. Cook, Biochemistry and Molecular Biology Education 33(3), 194-201 (2005))

Protein Function Associated reaction
Catalase Hydrogen peroxide disproportionation 2 H2O2 → 2 H2O + O2
Cytochrome c (cyt c) Electron transfer Fe(II)-cyt c ⇌ Fe(III)-cyt c + e-
Myoglobin (Mb) Reversible O2 binding in muscle Mb + O2 ⇌ MbO2

Protein 1


Protein 2

Protein 3

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