|
Descripción
|
|
|---|---|
| Hydrogenases mediate biological production and oxidation of hydrogen, two key energy relevant processes. The synthesis of these metalloenzymes requires a complex series of biochemical reactions to assemble protein subunits and metallic cofactors. In the case of NiFe hydrogenases, a final step in this biosynthetic pathway is the processing of a C-terminal tail (CTT) from the hydrogenase large subunit (LSU), a step required for the insertion of nickel in the unique NiFe(CN)2CO cofactor present in these enzymes. Results from in silica modelling and Molecular Dynamics (MD) analyses of processed vs. unprocessed forms of Rhizobium leguminosarum bv. viciae (Rlv) hydrogenase LSU indicate that its CTT behaves as an Intrinsically Disordered Region (IDR) that likely provides the required flexibility for the protein to interact with the protease during the final steps of proteolytic maturation. Prediction of pKa values of ionizable side chains in both forms of the enzyme?s large subunit also revealed that the presence of the CTT strongly modify the protonation state of some key residues around the active site. Two glutamate residues likely contributing to the process of nickel incorporation into the enzyme have been identified through MD simulations and its effect on enzyme maturation has been confirmed through mutant analysis (see Albareda et al., in this Conference). Computational analysis also revealed structural details on the interaction of Rlv HupL hydrogenase LSU with the endoprotease HupD responsible for the removal of CTT. | |
|
Internacional
|
Si |
|
Nombre congreso
|
International conference on Hydrogenases |
|
Tipo de participación
|
970 |
|
Lugar del congreso
|
Lisboa |
|
Revisores
|
Si |
|
ISBN o ISSN
|
0000000000 |
|
DOI
|
|
|
Fecha inicio congreso
|
31/03/2019 |
|
Fecha fin congreso
|
04/04/2019 |
|
Desde la página
|
156 |
|
Hasta la página
|
157 |
|
Título de las actas
|
ICH2019 Book of Abstracts |