Hi,

I would expect that the principal issue is that (bis)mono and bidentate iron 
complexes are likely to have different chemistries, even though they would have 
the same number of oxygen atoms nearby the iron atom – For example, unlike two 
monodentate carboxylates, the shape of a bidentate carboxylate is unlikely to 
allow the oxygen atoms to coordinate in an idealised octahedral or tetrahedral 
orientation at the iron atom.

So I’d expect that metalloenzymes would simply evolve to have carboxylates with 
the correct denticity (or capacity to cycle between mono and bidentate) to 
catalyse their reactions.

Here’s an article that discusses this in one particular case of methane 
monooxygenase (with glutamates providing the carboxylate ligands)

Mikael A. Miniera  and   Stephen J. Lippard, Dalton Trans 2015, 44, 18111
DOI: 10.1039/C5DT02138C

Ian

From: CCP4 bulletin board <[email protected]> On Behalf Of Chandra Prakash 
Tiwari
Sent: 18 July 2019 17:07
To: [email protected]
Subject: [ccp4bb] Bidentate GLU vs two monodentate GLU in metalloproteins

[EXTERNAL]
Dear all,
What is more preferable or conserved by evolution of lifeform point of view 
between glutamate acting as bidentate ligand by its carboxylate group or two 
monodentate GLU at metal binding site in natural metalloenzymes.
I was thinking 2 GLU are better than one bidentate GLU because if one GLU gets 
mutated other GLU will still be able to form a coordination bond to a metal.
Please comment and help if i am right or wrong. metal is Fe2+. In short which 
will evolve with time a bidentate GLU or 2 monodentate GLU.

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