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

Publikováno v: 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
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Biochimica biophysica acta (BBA)-Bioenergetics, 2015, 1847 (2), pp.162-170. ⟨10.1016/j.bbabio.2014.06.011⟩

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 tu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8703f353ab83acb29b8d528d3aebaa72

Introduction of Methionines in the Gas Channel Makes [NiFe] Hydrogenase Aero-Tolerant

Autor: Laurent Cournac, Michael Haumann, Anne Volbeda, Antonio L. De Lacey, Fanny Leroux, Bénédicte Burlat, Sébastien Dementin, Marc Rousset, Lydie Martin, Oliver Sanganas, Juan C. Fontecilla-Camps, Victor M. Fernandez, Bruno Guigliarelli, Stéphanie Champ, Christophe Léger, Nicolas Martinez

Publikováno v: Journal of the American Chemical Society. 131:10156-10164

Hydrogenases catalyze the conversion between 2H(+) + 2e(-) and H(2)(1). Most of these enzymes are inhibited by O(2), which represents a major drawback for their use in biotechnological applications. Improving hydrogenase O(2) tolerance is therefore a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a26c7e62e62db0fbfe354cad404ad24
https://doi.org/10.1021/ja9018258

[NiFe] and [FeS] cofactors in the membrane-bound hydrogenase of Ralstonia eutropha investigated by X-ray absorption spectroscopy: Insights into O 2-tolerant H2 cleavage

Autor: Holger Dau, Johannes Fritsch, Antonio L. De Lacey, Matthias Stein, Elisabeth Siebert, Bärbel Friedrich, Oliver Lenz, Ingo Zebger, Marcus Ludwig, Oliver Sanganas, Simone Löscher, Michael Haumann

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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Molecular features that allow certain [NiFe] hydrogenases to catalyze the conversion of molecular hydrogen (H2) in the presence of dioxygen (O2) were investigated. Using X-ray absorption spectroscopy (XAS), we compared the [NiFe] active site and FeS

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc318d41f874b8106f44dd1e2198bdca
http://hdl.handle.net/10261/80644

How oxygen attacks [FeFe] hydrogenases from photosynthetic organisms

Autor: Thomas Happe, Oliver Sanganas, Kylie A. Vincent, Caterina Brandmayr, Fraser A. Armstrong, Sven T. Stripp, Gabrielle Goldet, Michael Haumann

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 106(41)

Green algae such as Chlamydomonas reinhardtii synthesize an [FeFe] hydrogenase that is highly active in hydrogen evolution. However, the extreme sensitivity of [FeFe] hydrogenases to oxygen presents a major challenge for exploiting these organisms to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f27af60af97fa5dce2d6630a171abb3
http://ora.ox.ac.uk/objects/uuid:4193fa71-2b05-4f96-ae4c-22a93d081cfd

Redox intermediates of the Mn-Fe Site in subunit R2 of Chlamydia trachomatis ribonucleotide reductase: an X-ray absorption and EPR study

Autor: Nina, Voevodskaya, Friedhelm, Lendzian, Oliver, Sanganas, Alexander, Grundmeier, Astrid, Gräslund, Michael, Haumann

Publikováno v: The Journal of biological chemistry. 284(7)

The R2 protein of class I ribonucleotide reductase (RNR) from Chlamydia trachomatis (Ct) can contain a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::87cf9ffc4ccbe89b274c6caaee1593fd
https://pubmed.ncbi.nlm.nih.gov/19095645