Premium
Reactivation pathway of the hydrogenase H‐cluster: Density functional theory study
Author(s) -
Motiu Stefan,
Dogaru Daniela,
Gogonea Valentin
Publication year - 2006
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.21236
Subject(s) - chemistry , density functional theory , protonation , cluster (spacecraft) , hydrogenase , ligand (biochemistry) , ruthenium , amine gas treating , metal , active site , stereochemistry , crystallography , computational chemistry , catalysis , organic chemistry , biochemistry , ion , receptor , computer science , programming language
This work puts forth a reaction pathway for the reactivation of exogenous ligand inhibited H‐cluster, the active site of Fe‐only hydrogenases. The H‐cluster is a dimetal complex, Fe–Fe, with the metal centers bridged by di(thiomethyl)amine. Exogenous ligands, H 2 O, and OH − , are bound to the distal iron (Fe d ). Density functional theory (DFT) calculations on the native and ruthenium‐modified H‐cluster have been performed using the B3LYP functional with 6‐31+G** and 6‐311+G** basis sets. We have ascertained that there is a thermodynamically favorable pathway for the reactivation of the OH − inhibited H‐cluster, which proceeds by an initial protonation of the Fe d –OH − complex. The proposed reaction pathway has all its intermediate reactions ensue exothermically. © 2006 Wiley Periodicals, Inc. Int J Quantum Chem, 2007