M
Matthias Stein
Researcher at Max Planck Society
Publications - 137
Citations - 3554
Matthias Stein is an academic researcher from Max Planck Society. The author has contributed to research in topics: Catalysis & Active site. The author has an hindex of 34, co-authored 126 publications receiving 3140 citations. Previous affiliations of Matthias Stein include Free University of Berlin & Technical University of Berlin.
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Journal ArticleDOI
A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase
Tobias Goris,Annemarie F. Wait,Miguel Saggu,Johannes Fritsch,Nina Heidary,Matthias Stein,Ingo Zebger,Friedhelm Lendzian,Fraser A. Armstrong,Bärbel Friedrich,Oliver Lenz +10 more
TL;DR: The data indicate that the mechanism of O(2) tolerance relies on the reductive removal of oxygenic species guided by the unique architecture of the electron relay rather than a restricted access of O (2) to the active site.
Journal ArticleDOI
Single crystal EPR studies of the reduced active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F.
TL;DR: The calculated g tensor of Ni-C is in good agreement with the experimental one for a formal Ni(III) oxidation state with a hydride (H(-)) bridge between the Ni and the Fe atom, and satisfied agreement is obtained for the Ni-L state.
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A Model of the [FeFe] Hydrogenase Active Site with a Biologically Relevant Azadithiolate Bridge: A Spectroscopic and Theoretical Investigation
Oezlen F. Erdem,Lennart Schwartz,Matthias Stein,Alexey Silakov,Sandeep Kaur-Ghumaan,Ping Huang,Sascha Ott,Edward J. Reijerse,Wolfgang Lubitz +8 more
TL;DR: Convincing evidence for the presence of a nitrogen atom in the dithiolate bridge of the active site of native [FeFe] hydrogenases (B) is provided by a spectroscopic, electrochemical, and theoretica study.
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Catalytic hydrogen evolution from mononuclear iron(II) carbonyl complexes as minimal functional models of the [FeFe] hydrogenase active site.
TL;DR: How much iron does it take?
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Ligand versus metal protonation of an iron hydrogenase active site mimic
Gerriet Eilers,Lennart Schwartz,Matthias Stein,Giuseppe Zampella,Luca De Gioia,Sascha Ott,Reiner Lomoth +6 more
TL;DR: The protonation behavior of the iron hydrogenase active-site mimic [Fe2(mu-adt)(CO)4(PMe3)2] (1; adt=N-benzyl-azadithiolate) has been investigated by spectroscopic, electrochemical, and computational methods.