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EC Number Crystallization (Commentary)
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6-
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6hanging drop vapor diffusion method
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6in complex with an iron guanylyl pyridone,
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6mutant C176A crystallized in the presence of dithiothreitol, at 1.95 A resolution
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6sitting drop vapor diffusion method
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6sitting drop vapor diffusion technique, the crystal structure of recombinant enzyme is solved to a maximum resolution of 1.5 A (reduced) or 2.2 A (as-isolated)
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6theoretical 3D strucutural model. For the wild-type, the hydrogen bond of the network involving H82 and the bridging cysteines is formed with the sulfur atom of C78 whereas for the C81S mutant, it is formed with the bridging sulfur atom from C600. Calculations indicate a water molecule close to C81, which influences the IR spectra
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6to 1.5 A resolution. The heterodimeric enzyme consists of a large subunit harbouring the catalytic centre in the H2-reduced state and a small subunit containing an electron relay consisting of three different iron-sulfur clusters. The cluster proximal to the active site displays an unprecedented [4Fe-3S] structure and is coordinated by six cysteines. According to the current model, this cofactor operates as an electronic switch depending on the nature of the gas molecule approaching the active site. It serves as an electron acceptor in the course of H2 oxidation and as an electron-delivering device upon O2 attack at the active site
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6to 3.3 A resolution, in a 2:1 complex with its physiological partner, cytochrome b. From the short distance between distal [Fe4S4] clusters, a rapid transfer of H2-derived electrons between hydrogenase heterodimers is predicted. Thus, under low O2 levels, a functional active site in one heterodimer can reductively reactivate its O2-exposed counterpart in the other
Show all pathways known for 1.12.99.6Display the word mapDisplay the reaction diagram Show all sequences 1.12.99.6[NiFe] hydrogenase has two different oxidized states, Ni-A (unready, exhibits a lag phase in reductive activation) and Ni-B (ready). Conversion of Ni-B to Ni-A with the use of Na2S and O2 and determination of the high-resolution crystal structures of both states
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