Modulation of active site electronic structure by the protein matrix to control [NiFe] hydrogenase reactivity

Dayle M A Smith, Simone Raugei, Thomas C. Squier

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Control of the reactivity of the nickel center of the [NiFe] hydrogenase and other metalloproteins commonly involves outer coordination sphere ligands that act to modify the geometry and physical properties of the active site metal centers. We carried out a combined set of classical molecular dynamics and quantum/classical mechanics calculations to provide quantitative estimates of how dynamic fluctuations of the active site within the protein matrix modulate the electronic structure at the catalytic center. Specifically we focused on the dynamics of the inner and outer coordination spheres of the cysteinate-bound Ni-Fe cluster in the catalytically active Ni-C state. There are correlated movements of the cysteinate ligands and the surrounding hydrogen-bonding network, which modulate the electron affinity at the active site and the proton affinity of a terminal cysteinate. On the basis of these findings, we hypothesize a coupling between protein dynamics and electron and proton transfer reactions critical to dihydrogen production.

Original languageEnglish
Pages (from-to)24026-24033
Number of pages8
JournalPhysical Chemistry Chemical Physics
Volume16
Issue number43
DOIs
Publication statusPublished - Nov 21 2014

Fingerprint

Electronic structure
reactivity
Modulation
electronic structure
proteins
modulation
matrices
Metalloproteins
Ligands
Electron affinity
ligands
Proteins
Proton transfer
protons
classical mechanics
electron affinity
Nickel
affinity
Molecular dynamics
Protons

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Physics and Astronomy(all)

Cite this

Modulation of active site electronic structure by the protein matrix to control [NiFe] hydrogenase reactivity. / Smith, Dayle M A; Raugei, Simone; Squier, Thomas C.

In: Physical Chemistry Chemical Physics, Vol. 16, No. 43, 21.11.2014, p. 24026-24033.

Research output: Contribution to journalArticle

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