COMP 339 |
| It is economically imperative to engineer [FeFe]-hydrogenases (from Desulfovibrio desulfuricans) to function aerobically and to yield H2. One way to achieve this is through computational studies using quantum mechanics (DFT) and molecular mechanics (MM) calculations. From previous work[1], it was found that the oxidation of [FeFe]-hydrogenase active site (H-cluster) is reversible. ONIOM results agree with experimental results[2] showing that the enzyme is inhibited in the H2O removal step (ÄH(frozen enzyme.) = +24.89kcal/mol, and ÄH(unfrozen. enzyme.) = +19.60 kcal/mol). The current investigation probes the potential inhibitory site whence the H2O-retention feedback mechanism occurs. The H-cluster juxtaposed amino acids are the plausible candidates for the H2O-retention command[3]. The first step is identifying which H-cluster proximal amino acid is involved in the H2O-retention command. This consists of sequentially switching off the amino acids' charges, followed by ONIOM calculations. Once the key amino acid has been identified, conservative mutations are carried out on it. [1] Motiu, S.; Dogaru, D.; Gogonea, V. Int. J. Quantum Chem. 2006, 107, 1248-1252 [2] Peters, J. W.; Lanzilotta, W. N.; Lemon, B. J.; Seefeldt, L. C. Science 1998, 282, 1853-1858. [3] Nicolet, Y.; Piras, C.; Legrand, P.; Hatchikian, E. C.; Fontecilla-Camps, J. C. Structure 1999, 7, 13-23 |
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Poster Session
6:00 PM-8:00 PM, Tuesday, August 21, 2007 BCEC -- Ballroom Foyer, Poster
Sci-Mix
Division of Computers in Chemistry |