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ACS: Take a walk on the wild side

My background is in organic chemistry, but the great thing about a meeting like this is that I can learn new things. So yesterday, I decided to explore the strange (to me) world of inorganic chemistry. Frankly, I had no idea what I would discover. I half expected the inorganic attendees to fall silent when I walked into the room, staring at me with hostile eyes, before announcing "We don't like organic chemists in these parts". I think the jetlag is making me paranoid.

But no, it was all cool and I saw some great stuff. Naively, I would never have expected to see an enzyme crystal structure outside of a drug discovery seminar. But then I discovered bioinorganic chemistry, and there were active sites everywhere. John Lipscomb and Steve Lippard gave some cracking talks about the metal species found in enzymes, such as Rieske dioxygenases and bacterial multicomponent monooxgenases. These proteins can be thought of as the original C-H activation specialists. On a similar vein, Thomas Rauchfuss is doing some amazing chemistry to model the active site of hydrogenases.

What I really liked about these sessions was that the lecture rooms were smaller (it was standing room only for Lippard's talk), and the debate was lively. Every talk inspired interesting discussion, and I was impressed by the spirit of academic engagement, which I hadn't really encountered elsewhere. So, if you're sticking closely to your own areas, why not go foraging in foreign territory? You might like what you find.

Andy

Andrew Mitchinson (Associate Editor, Nature)

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If inorganikers want ligands they need organikers. If organikers want reagents they need inorganikers. That organikers make do with one element and inorganikers require the whole Periodic Table to remain employed is merely a matter of... gaping in horror at biochemists.

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