Sandbox 181: Difference between revisions

Line 21:

==Compression and Hydride Transfer==

Compression has been shown to play a role in enzyme catalysis and X-ray structure of NADPH complex of GSH reductase shows the C4 atom to be only 3.3 Angstrom from the flavin N5 atom<ref name="main"/>. This is closer than one would predict with van der Waals interactions. Compression of the NADPH-bound complex is first evidenced in the decrease in the level of motion of the active site atoms in the complex<ref name="main"/>. Second, it was observed that the van der Waals radii overlapped in the active site, tightly fixing flavin<ref name="main"/>. It is ~~tightly~~ fixed from both sides as flavin N5 to nicotinamide C4 distance is 3.29 Angstrom and the flavin C4a to Cys63-SG distance is 3.29 Angstrom <ref name="main"/>. Third, the flavin ring system shifts in the two reduced structures, with the binding of NADPH pushing the flavin N5 about 0.3 Angstrom towards the thiolate<ref name="main"/>. This provides a structural explanation for how the thiolate-flavin charge transfer intensity is increased by the binding of NADPH <ref name="main"/>. Finally, the last evidence for compression involves the planarity of the nicotinamide group which shows distortion at atom N1 <ref name="main"/>.

Compression has been shown to play a role in enzyme catalysis and X-ray structure of NADPH complex of GSH reductase shows the C4 atom to be only 3.3 Angstrom from the flavin N5 atom<ref name="main"/>. This is closer than one would predict with van der Waals interactions. Compression of the NADPH-bound complex is first evidenced in the decrease in the level of motion of the active site atoms in the complex<ref name="main"/>. Second, it was observed that the van der Waals radii overlapped in the active site, tightly fixing flavin<ref name="main"/>. It is fixed from both sides as flavin N5 to nicotinamide C4 distance is 3.29 Angstrom and the flavin C4a to Cys63-SG distance is 3.29 Angstrom <ref name="main"/>. Third, the flavin ring system shifts in the two reduced structures, with the binding of NADPH pushing the flavin N5 about 0.3 Angstrom towards the thiolate<ref name="main"/>. This provides a structural explanation for how the thiolate-flavin charge transfer intensity is increased by the binding of NADPH <ref name="main"/>. Finally, the last evidence for compression involves the planarity of the nicotinamide group which shows distortion at atom N1 <ref name="main"/>.

=Reaction=

Sandbox 181: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 21: / Line 21: @@
 ==Compression and Hydride Transfer==
-Compression has been shown to play a role in enzyme catalysis and X-ray structure of NADPH complex of GSH reductase shows the C4 atom to be only 3.3 Angstrom from the flavin N5 atom<ref name="main"/>. This is closer than one would predict with van der Waals interactions. Compression of the NADPH-bound complex is first evidenced in the decrease in the level of motion of the active site atoms in the complex<ref name="main"/>. Second, it was observed that the van der Waals radii overlapped in the active site, tightly fixing flavin<ref name="main"/>. It is tightly fixed from both sides as flavin N5 to nicotinamide C4 distance is 3.29 Angstrom and the flavin C4a to Cys63-SG distance is 3.29 Angstrom <ref name="main"/>. Third, the flavin ring system shifts in the two reduced structures, with the binding of NADPH pushing the flavin N5 about 0.3 Angstrom towards the thiolate<ref name="main"/>. This provides a structural explanation for how the thiolate-flavin charge transfer intensity is increased by the binding of NADPH <ref name="main"/>. Finally, the last evidence for compression involves the planarity of the nicotinamide group which shows distortion at atom N1 <ref name="main"/>.
+Compression has been shown to play a role in enzyme catalysis and X-ray structure of NADPH complex of GSH reductase shows the C4 atom to be only 3.3 Angstrom from the flavin N5 atom<ref name="main"/>. This is closer than one would predict with van der Waals interactions. Compression of the NADPH-bound complex is first evidenced in the decrease in the level of motion of the active site atoms in the complex<ref name="main"/>. Second, it was observed that the van der Waals radii overlapped in the active site, tightly fixing flavin<ref name="main"/>. It is fixed from both sides as flavin N5 to nicotinamide C4 distance is 3.29 Angstrom and the flavin C4a to Cys63-SG distance is 3.29 Angstrom <ref name="main"/>. Third, the flavin ring system shifts in the two reduced structures, with the binding of NADPH pushing the flavin N5 about 0.3 Angstrom towards the thiolate<ref name="main"/>. This provides a structural explanation for how the thiolate-flavin charge transfer intensity is increased by the binding of NADPH <ref name="main"/>. Finally, the last evidence for compression involves the planarity of the nicotinamide group which shows distortion at atom N1 <ref name="main"/>.
 =Reaction=