Structural differences of oxidized iron–sulfur and nickel–iron cofactors in O2-tolerant and O2-sensitive hydrogenases studied by X-ray absorption spectroscopy

Autor: Oliver Lenz, Hirofumi Nishihara, Petko Chernev, Fraser A. Armstrong, Nils Leidel, Kajsa G.V. Sigfridsson, Marc Rousset, Antonio L. De Lacey, Ki Seok Yoon, Oliver Sanganas, Michael Haumann, Sébastien Dementin, Alison Parkin
Přispěvatelé: Lund University [Lund], Humboldt-Universität zu Berlin, Freie Universität Berlin, Konkuk University, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Tokyo Institute of Technology [Tokyo] (TITECH), Department of Chemistry [York, UK], University of York [York, UK], Inorganic Chemistry Laboratory [Oxford], University of Oxford [Oxford], Bioénergétique et Ingénierie des Protéines (BIP ), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU), Centro de Investigaciones Biológicas (CSIC), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), German Research Foundation, Röntgen-Ångström Cluster, Ministerio de Economía y Competitividad (España), Royal Society (UK), Humboldt University Of Berlin, Konkuk University [Seoul], University of Oxford, Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2015
Předmět:
Zdroj: Biochimica biophysica acta (BBA)-Bioenergetics
Biochimica biophysica acta (BBA)-Bioenergetics, Elsevier, 2015, 1847 (2), pp.162-170. ⟨10.1016/j.bbabio.2014.06.011⟩
Digital.CSIC. Repositorio Institucional del CSIC
instname
Biochimica biophysica acta (BBA)-Bioenergetics, 2015, 1847 (2), pp.162-170. ⟨10.1016/j.bbabio.2014.06.011⟩
ISSN: 0005-2728
1879-2650
DOI: 10.1016/j.bbabio.2014.06.011
Popis: The class of [NiFe]-hydrogenases comprises oxygen-sensitive periplasmic (PH) and oxygen-tolerant membrane-bound (MBH) enzymes. For three PHs and four MBHs from six bacterial species, structural features of the nickel–iron active site of hydrogen turnover and of the iron–sulfur clusters functioning in electron transfer were determined using X-ray absorption spectroscopy (XAS). Fe-XAS indicated surplus oxidized iron and a lower number of ~ 2.7 Å Fe–Fe distances plus additional shorter and longer distances in the oxidized MBHs compared to the oxidized PHs. This supported a double-oxidized and modified proximal FeS cluster in all MBHs with an apparent trimer-plus-monomer arrangement of its four iron atoms, in agreement with crystal data showing a [4Fe3S] cluster instead of a [4Fe4S] cubane as in the PHs. Ni-XAS indicated coordination of the nickel by the thiol group sulfurs of four conserved cysteines and at least one iron–oxygen bond in both MBH and PH proteins. Structural differences of the oxidized inactive [NiFe] cofactor of MBHs in the Ni-B state compared to PHs in the Ni–A state included a ~ 0.05 Å longer Ni-O bond, a two times larger spread of the Ni–S bond lengths, and a ~ 0.1 Å shorter Ni–Fe distance. The modified proximal [4Fe3S] cluster, weaker binding of the Ni–Fe bridging oxygen species, and an altered localization of reduced oxygen species at the active site may each contribute to O2 tolerance.
M.H. thanks the Deutsche Forschungsgemeinschaft (DFG) for a Heisenberg Fellowship and the DFG (grants Ha3265/3-1 and Ha3265/6-1) and the Bundesministerium für Bildung und Wissenschaft (grant 05K14KE1 within the Röntgen-Angström Cluster) for the financial support. A.L.D.L thanks MINECO (project CTQ2012-32448) for the financial support. F.A.A. is a Royal Society Wolfson Research Merit Award holder.
Databáze: OpenAIRE
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