Measurement and ab initio calculation of CSA/dipole-dipole cross-correlated relaxation provide insight into the mechanism of a H2-forming dehydrogenase.
Using transferred cross-correlated relaxation and DFT calculations, the conformation of the relevant conformation of N5,N10-methylenetetrahydromethanopterin, a reaction intermediate bound to the 80 kD H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase is determined. The conformation of the intermediate differs from the free form in solution and makes the reaction mechanism plausible.
Max-Planck-Institut für terrestrische Mikrobiologie and Laboratorium für Mikrobiologie des Fachbereichs Biologie der Philipps-Universität, Karl-von-Frisch-Strasse, D-35043 Marburg, Germany.
Stefan
S
Bartoschek
Gerrit
G
Buurman
Bernhard H
BH
Geierstanger
Jon
J
Lapham
Christian
C
Griesinger
D017013:Methanobacteriaceae / Q000201:enzymology; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011622:Pterins / Q000737:chemistry / Q000378:metabolism
D011622:Pterins; C042416:5,6,7,8-tetrahydromethanopterin; D000587:Oxidoreductases Acting on CH-NH Group Donors; C047126:methylenetetrahydromethanopterin dehydrogenase