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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03206naa a2200397 4500 | |
| 001 | oai:lup.lub.lu.se:1f2c67f3-797b-45ef-b1ae-4d6bd55bfcda | |
| 003 | SwePub | |
| 008 | 160401s2011 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://lup.lub.lu.se/record/18685552 URI |
| 024 | 7 | a https://doi.org/10.1002/chem.2010014932 DOI |
| 040 | a (SwePub)lu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a art2 swepub-publicationtype |
| 072 | 7 | a ref2 swepub-contenttype |
| 100 | 1 | a Greco, Claudio4 aut |
| 245 | 1 0 | a Isocyanide in Biochemistry? A Theoretical Investigation of the Electronic Effects and Energetics of Cyanide Ligand Protonation in [FeFe]-Hydrogenases |
| 264 | c 2011-01-12 | |
| 264 | 1 | b Wiley,c 2011 |
| 520 | a The presence of Fe-bound cyanide ligands in the active site of the proton-reducing enzymes [FeFe]-hydrogenases has led to the hypothesis that such Bronsted-Lowry bases could be protonated during the catalytic cycle, thus implying that hydrogen isocyanide (HNC) might have a relevant role in such crucial microbial metabolic paths. We present a hybrid quantum mechanical/molecular mechanical (QM/MM) study of the energetics of CN- protonation in the enzyme, and of the effects that cyanide protonation can have on [FeFe]-hydrogenase active sites. A detailed analysis of the electronic properties of the models and of the energy profile associated with H-2 evolution clearly shows that such protonation is dysfunctional for the catalytic process. However, the inclusion of the protein matrix surrounding the active site in our QM/MM models allowed us to demonstrate that the amino acid environment was finely selected through evolution, specifically to lower the Bronsted-Lowry basicity of the cyanide ligands. In fact, the conserved hydrogen-bonding network formed by these ligands and the neighboring amino acid residues is able to impede CN- protonation, as shown by the fact that the isocyanide forms of [FeFe]-hydrogenases do not correspond to stationary points on the enzyme QM/MM potential-energy surface. | |
| 650 | 7 | a NATURVETENSKAPx Kemix Teoretisk kemi0 (SwePub)104072 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Chemical Sciencesx Theoretical Chemistry0 (SwePub)104072 hsv//eng |
| 653 | a density functional calculations | |
| 653 | a hydrogenases | |
| 653 | a isocyanide ligands | |
| 653 | a protonation | |
| 653 | a QM/MM methods | |
| 700 | 1 | a Bruschi, Maurizio4 aut |
| 700 | 1 | a Fantucci, Piercarlo4 aut |
| 700 | 1 | a Ryde, Ulfu Lund University,Lunds universitet,Beräkningskemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Computational Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)teok-ury |
| 700 | 1 | a De Gioia, Luca4 aut |
| 710 | 2 | a Beräkningskemib Enheten för fysikalisk och teoretisk kemi4 org |
| 773 | 0 | t Chemistry: A European Journald : Wileyg 17:6, s. 1954-1965q 17:6<1954-1965x 1521-3765x 0947-6539 |
| 856 | 4 | u http://dx.doi.org/10.1002/chem.201001493y FULLTEXT |
| 856 | 4 8 | u https://lup.lub.lu.se/record/1868555 |
| 856 | 4 8 | u https://doi.org/10.1002/chem.201001493 |
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