#chempaperaday Day 29/365: "Biosynthesis of the Urease Metallocenter"

I am dying to know how metalloproteins are "made" and folded in the cell. When do the metals take their places? How is the concentration of the metal ion is regulated? What kind of proteins or molecules helped them to enter the cell and how do they end up where they belong?

This article is a review about urease; a nickel containing metalloprotein.

http://www.jbc.org/content/288/19/13178

http://www.rcsb.org/pdb/explore/explore.do?structureId=1FWJ

#chempaperaday Day 25/365: "Designing Hydrolytic Zinc Metalloenzymes"

Zinc is one of the most common transition metal ions in biological systems. As you can expect, it is found as  Zn(II) and acts as a strong Lewis Acid providing strong binding interactions. It can be found in several proteins and I can list at least two of them without looking at any textbook: carbonic anhydrase and alcohol dehydrogenase. I can add the zinc fingers too. But, they are not proteins although they can be found in several proteins. 

Actually 6 months ago, I made an animation on PyMOL about carbonic anhydrase II and here it is:

I tried to link my youtube video, but it didn't work. Instead I uploaded the original file. Hope that works.

Today I am reading a great review on zinc metalloenzymes and to be honest I haven't finished reading yet. But, it will be over by midnight. I hope you enjoy it.

http://pubs.acs.org/doi/abs/10.1021%2Fbi4016617

DOI: 10.1021/bi4016617

#chempaperaday Day 10/365: "Metal-based anticancer drugs: From a past anchored in platinum chemistry to a post-genomic future of diverse chemistry and biology"

More metal based antitumor complexes? This is a short but good review on them. It is free to read.

Here I used PyMOL to see how cisplatin kinks the duplex by binding DNA in a covalent manner. Its color is magenta (the one on the right). I tried my best but it is really hard to see.

http://www.rcsb.org/pdb/explore/explore.do?structureId=1AIO

http://www.nature.com/nature/journal/v377/n6550/abs/377649a0.html

Myoglobin

Myoglobin is a very common protein in red blood cells. Its "duty" is to store oxygen and only under extreme conditions it releases the oxygen. So, it has a higher affinity for oxygen than hemoglobin has. It is almost identical to a single unit of hemoglobin. Anyway, I will not go into details and if you want to learn more about it, you can just read a Biochemistry textbook or even google it.

Another reason why it is a special protein is that it was the first protein that was "solved." After years of work, John Kendrew and his team finally solved the structure of the protein and built a model. Below is the model and I have learned that you can visit it at Science Museum in London. Unfortunately, it looks disgusting. I wish they had chosen a better color and material to build the model.

http://www.sciencemuseum.org.uk/images/i053/10321094.aspx

And here is a model generated by PyMOL on my laptop. It looks cute now: