Reaction Coordinate Leading to H Production in [FeFe]-Hydrogenase Identified by Nuclear Resonance Vibrational Spectroscopy and Density Functional Theory.
[FeFe]-hydrogenases are metalloenzymes that reversibly reduce protons to molecular hydrogen at exceptionally high rates. We have characterized the catalytically competent hydride state (H) in the [FeFe]-hydrogenases from both Chlamydomonas reinhardtii and Desulfovibrio desulfuricans using Fe nuclear...
| Publicado en: | Journal of the American Chemical Society Vol. 139; no. 46; pp. 16894 - 16903 |
|---|---|
| Autores principales: | , , , , , , , , , , , , |
| Formato: | Artículo |
| Publicado: |
American Chemical Society
11/22/2017
|
| Materias: | |
| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=126507548&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 126507548 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 11/22/2017 vid: 139 iid: 46 pid: 997 pub: American Chemical Society artinfo: ui: 126507548 10.1021/jacs.7b09751 ppf: 16894 ppct: 9 formats: tig: atl: Reaction Coordinate Leading to H Production in [FeFe]-Hydrogenase Identified by Nuclear Resonance Vibrational Spectroscopy and Density Functional Theory. aug: au: Pelmenschikov, Vladimir Birrell, James A. Pham, Cindy C. Mishra, Nakul Hongxin Wang Sommer, Constanze Reijerse, Edward Richers, Casseday P. Tamasaku, Kenji Yoda, Yoshitaka Rauchfuss, Thomas B. Lubitz, Wolfgang Cramer, Stephen P. affil: Institut fur Chemie, Technische Universitat Berlin, Strasse des 17 Juni 135, 10623 Berlin, Germany Max-Planck-Institut fur Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mulheim an der Ruhr, Germany Department of Chemistry, University of California, Davis, One Shields Avenue, Davis, California 95616, United States School of Chemical Sciences, University of Illinois, 600 S. Mathews Avenue, Urbana, Illinois 61801, United States JASRI, Spring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5198, Japan su: Hydrogen bonding Density functional theory Hydrogenase Chlamydomonas reinhardtii Desulfovibrio desulfuricans Chemical reactions Catalysis sug: subj: Hydrogen bonding Density functional theory Hydrogenase Chlamydomonas reinhardtii Desulfovibrio desulfuricans Chemical reactions Catalysis ab: [FeFe]-hydrogenases are metalloenzymes that reversibly reduce protons to molecular hydrogen at exceptionally high rates. We have characterized the catalytically competent hydride state (H) in the [FeFe]-hydrogenases from both Chlamydomonas reinhardtii and Desulfovibrio desulfuricans using Fe nuclear resonance vibrational spectroscopy (NRVS) and density functional theory (DFT). H/D exchange identified two Fe-H bending modes originating from the binuclear iron cofactor. DFT calculations show that these spectral features result from an iron-bound terminal hydride, and the Fe-H vibrational frequencies being highly dependent on interactions between the amine base of the catalytic cofactor with both hydride and the conserved cysteine terminating the proton transfer chain to the active site. The results indicate that H is the catalytic state one step prior to H2 formation. The observed vibrational spectrum, therefore, provides mechanistic insight into the reaction coordinate for H2 bond formation by [FeFe]-hydrogenases. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2017 holdings: @attributes: islocal: N |
|---|