How iron-containing proteins control dioxygen chemistry: a detailed atomic level description via accurate quantum chemical and mixed quantum mechanics/molecular mechanics calculations

Cited 55 time in webofscience Cited 66 time in scopus
  • Hit : 259
  • Download : 0
Over the past several years, rapid advances in computational hardware, quantum chemical methods, and mixed quantum mechanics/molecular mechanics (QM/MM) techniques have made it possible to model accurately the interaction of ligands with metal-containing proteins at an atomic level of detail. In this paper, we describe the application of our computational methodology, based on density functional (DFT) quantum chemical methods, to two diiron-containing proteins that interact with dioxygen: methane monooxygenase (MMO) and hemerythrin (Hr). Although the active sites are structurally related, the biological function differs substantially. MMO is an enzyme found in methanotrophic bacteria and hydroxylates aliphatic C-H bonds, whereas Hr is a carrier protein for dioxygen used by a number of marine invertebrates. Quantitative descriptions of the structures and energetics of key intermediates and transition states involved in the reaction with dioxygen are provided, allowing their mechanisms to be compared and contrasted in detail. An in-depth understanding of how the chemical identity of the first ligand coordination shell, structural features, electrostatic and van der Waals interactions of more distant shells control ligand binding and reactive chemistry is provided, affording a systematic analysis of how iron-containing proteins process dioxygen. Extensive contact with experiment is made in both systems, and a remarkable degree of accuracy and robustness of the calculations is obtained from both a qualitative and quantitative perspective. (C) 2002 Published by Elsevier Science B.V.
Publisher
ELSEVIER SCIENCE SA
Issue Date
2003-03
Language
English
Article Type
Review
Keywords

SOLUBLE METHANE MONOOXYGENASE; DENSITY-FUNCTIONAL THEORY; METHYLOCOCCUS-CAPSULATUS BATH; METHYLOSINUS-TRICHOSPORIUM OB3B; EFFECTIVE CORE POTENTIALS; C-H BOND; MOLECULAR-DYNAMICS SIMULATIONS; CONTINUUM DIELECTRIC THEORY; ELECTRON-TRANSFER REACTIONS; X-RAY ABSORPTION

Citation

COORDINATION CHEMISTRY REVIEWS, v.238, pp.267 - 290

ISSN
0010-8545
DOI
10.1016/S0010-8545(02)00284-9
URI
http://hdl.handle.net/10203/203367
Appears in Collection
CH-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 55 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0