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Vibrational Perturbation of the [FeFe] Hydrogenase H-Cluster Revealed by 13C2H-ADT Labeling.
Pelmenschikov, Vladimir; Birrell, James A; Gee, Leland B; Richers, Casseday P; Reijerse, Edward J; Wang, Hongxin; Arragain, Simon; Mishra, Nakul; Yoda, Yoshitaka; Matsuura, Hiroaki; Li, Lei; Tamasaku, Kenji; Rauchfuss, Thomas B; Lubitz, Wolfgang; Cramer, Stephen P.
Afiliação
  • Pelmenschikov V; Institut für Chemie, Technische Universität Berlin, 10623 Berlin, Germany.
  • Birrell JA; Max Planck Institute for Chemical Energy Conversion, 45470 Mülheim an der Ruhr, Germany.
  • Gee LB; Department of Chemistry, Stanford University, Stanford, California 94305, United States.
  • Richers CP; School of Chemical Sciences, University of Illinois, Urbana, Illinois 61801, United States.
  • Reijerse EJ; Max Planck Institute for Chemical Energy Conversion, 45470 Mülheim an der Ruhr, Germany.
  • Wang H; SETI Institute, Mountain View, California 94043, United States.
  • Arragain S; IFP Energies nouvelles, 92852 Rueil-Malmaison, France.
  • Mishra N; Department of Chemistry, University of California, Davis, California 95616, United States.
  • Yoda Y; Department of Chemistry, University of California, Davis, California 95616, United States.
  • Matsuura H; Precision Spectroscopy Division, SPring-8/JASRI, Sayo, Hyogo 679-5198, Japan.
  • Li L; Life Science Research Infrastructure Group, Advanced Photon Technology Division, RIKEN/SPring-8 Center, Sayo, Hyogo 679-5148, Japan.
  • Tamasaku K; Hyogo Science and Technology Association, Synchrotron Radiation Research Center, Tatsuno-shi, Hyogo 679-5165, Japan.
  • Rauchfuss TB; Research and Utilization Division, SPring-8/JASRI, Sayo, Hyogo 679-5198, Japan.
  • Lubitz W; School of Chemical Sciences, University of Illinois, Urbana, Illinois 61801, United States.
  • Cramer SP; Max Planck Institute for Chemical Energy Conversion, 45470 Mülheim an der Ruhr, Germany.
J Am Chem Soc ; 143(22): 8237-8243, 2021 06 09.
Article em En | MEDLINE | ID: mdl-34043346
[FeFe] hydrogenases are highly active catalysts for the interconversion of molecular hydrogen with protons and electrons. Here, we use a combination of isotopic labeling, 57Fe nuclear resonance vibrational spectroscopy (NRVS), and density functional theory (DFT) calculations to observe and characterize the vibrational modes involving motion of the 2-azapropane-1,3-dithiolate (ADT) ligand bridging the two iron sites in the [2Fe]H subcluster. A -13C2H2- ADT labeling in the synthetic diiron precursor of [2Fe]H produced isotope effects observed throughout the NRVS spectrum. The two precursor isotopologues were then used to reconstitute the H-cluster of [FeFe] hydrogenase from Chlamydomonas reinhardtii (CrHydA1), and NRVS was measured on samples poised in the catalytically crucial Hhyd state containing a terminal hydride at the distal Fe site. The 13C2H isotope effects were observed also in the Hhyd spectrum. DFT simulations of the spectra allowed identification of the 57Fe normal modes coupled to the ADT ligand motions. Particularly, a variety of normal modes involve shortening of the distance between the distal Fe-H hydride and ADT N-H bridgehead hydrogen, which may be relevant to the formation of a transition state on the way to H2 formation.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Hidrogênio / Hidrogenase / Proteínas Ferro-Enxofre Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Hidrogênio / Hidrogenase / Proteínas Ferro-Enxofre Idioma: En Ano de publicação: 2021 Tipo de documento: Article