M. Horch

发表

Domain motions and electron transfer dynamics in 2Fe-superoxide reductase.

P. Hildebrandt, I. Zebger, M. Horch, 2016, Physical chemistry chemical physics : PCCP.

Probing the active site of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 by in situ EPR and FTIR spectroscopy.

O. Lenz, P. Hildebrandt, I. Zebger, 2010, Angewandte Chemie.

Electrochemical and Infrared Spectroscopic Studies Provide Insight into Reactions of the NiFe Regulatory Hydrogenase from Ralstonia eutropha with O2 and CO.

O. Lenz, K. Vincent, I. Zebger, 2015, The journal of physical chemistry. B.

The Hydrogenase Subcomplex of the NAD+‐Reducing [NiFe] Hydrogenase from Ralstonia eutropha – Insights into Catalysis and Redox Interconversions

O. Lenz, K. Vincent, M. Haumann, 2011 .

Rational redox tuning of transition metal sites: learning from superoxide reductase.

M. Horch, 2019, Chemical communications.

An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2 -Tolerant Hydrogenase.

M. Driess, I. Zebger, Shenglai Yao, 2017, Angewandte Chemie.

Metal-induced histidine deprotonation in biocatalysis? Experimental and theoretical insights into superoxide reductase

M. Teixeira, P. Hildebrandt, I. Zebger, 2014 .

Exploring Structure and Function of Redox Intermediates in [NiFe]‐Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes

K. Tamasaku, S. Frielingsdorf, O. Lenz, 2021, Angewandte Chemie.

Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution† †Electronic supplementary information (ESI) available: Complementary resonance Raman and infrared spectroscopic data. See DOI: 10.1039/c6sc01098a Click here for additional data file.

P. Hildebrandt, I. Zebger, T. Happe, 2016, Chemical science.

Reversible active site sulfoxygenation can explain the oxygen tolerance of a NAD+-reducing [NiFe] hydrogenase and its unusual infrared spectroscopic properties.

O. Lenz, P. Hildebrandt, I. Zebger, 2015, Journal of the American Chemical Society.

Combining spectroscopy and theory to evaluate structural models of metalloenzymes: a case study on the soluble [NiFe] hydrogenase from Ralstonia eutropha.

P. Hildebrandt, I. Zebger, M. Horch, 2013, Chemphyschem : a European journal of chemical physics and physical chemistry.

Resonance Raman spectroscopy as a tool to monitor the active site of hydrogenases.

S. Frielingsdorf, O. Lenz, P. Hildebrandt, 2013, Angewandte Chemie.

Microporous polymer network films covalently bound to gold electrodes.

Arne Thomas, Johannes Schmidt, A. Fischer, 2015, Chemical communications.

Reversible Glutamate Coordination to High-Valent Nickel Protects the Active Site of a [NiFe] Hydrogenase from Oxygen.

G. M. Greetham, M. Ishii, O. Lenz, 2022, Journal of the American Chemical Society.

Impact of the iron-sulfur cluster proximal to the active site on the catalytic function of an O2-tolerant NAD(+)-reducing [NiFe]-hydrogenase.

O. Lenz, I. Zebger, L. Lauterbach, 2015, Biochemistry.

Enzymatic and spectroscopic properties of a thermostable [NiFe]‑hydrogenase performing H2-driven NAD+-reduction in the presence of O2.

O. Lenz, I. Zebger, S. Cramer, 2018, Biochimica et biophysica acta. Bioenergetics.

Understanding 2D-IR Spectra of Hydrogenases: A Descriptive and Predictive Computational Study

N. T. Hunt, M. Horch, Yvonne Rippers, 2022, Catalysts.

Concepts in bio-molecular spectroscopy: vibrational case studies on metalloenzymes.

P. Hildebrandt, I. Zebger, M. Horch, 2015, Physical chemistry chemical physics : PCCP.

Revealing the absolute configuration of the CO and CN- ligands at the active site of a [NiFe] hydrogenase.

P. Hildebrandt, I. Zebger, M. Horch, 2012, Chemphyschem : a European journal of chemical physics and physical chemistry.

NAD(H)‐coupled hydrogen cycling – structure–function relationships of bidirectional [NiFe] hydrogenases

O. Lenz, P. Hildebrandt, I. Zebger, 2012, FEBS letters.

Investigation of the NADH/NAD+ ratio in Ralstonia eutropha using the fluorescence reporter protein Peredox.

T. Friedrich, O. Lenz, I. Zebger, 2017, Biochimica et biophysica acta. Bioenergetics.

Reductive activation and structural rearrangement in superoxide reductase: a combined infrared spectroscopic and computational study.

M. Teixeira, P. Hildebrandt, I. Zebger, 2014, Physical chemistry chemical physics : PCCP.

Hydrogen evolution by cobalt hangman porphyrins under operating conditions studied by vibrational spectro-electrochemistry

I. Weidinger, K. Ly, P. Kielb, 2018 .

Shedding light on proton and electron dynamics in [FeFe] hydrogenases.

I. Zebger, T. Happe, C. Teutloff, 2020, Journal of the American Chemical Society.

Discriminating changes in intracellular NADH/NAD+ levels due to anoxicity and H2 supply in R. eutropha cells using the Frex fluorescence sensor.

T. Friedrich, O. Lenz, I. Zebger, 2019, Biochimica et biophysica acta. Bioenergetics.

Characterization of Frex as an NADH sensor for in vivo applications in the presence of NAD+ and at various pH values

T. Friedrich, O. Lenz, I. Zebger, 2017, Photosynthesis Research.

Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase

O. Lenz, P. Hildebrandt, A. Fischer, 2015, PloS one.

2nd coordination sphere controlled electron transfer of iron hangman complexes on electrodes probed by surface enhanced vibrational spectroscopy

I. Weidinger, N. Heidary, M. Schwalbe, 2015, Chemical science.

X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases

S. Shima, H. Dobbek, I. Zebger, 2019, Angewandte Chemie.

Nuclear resonance vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an O2-tolerant NAD+-reducing [NiFe] hydrogenase

O. Lenz, I. Zebger, S. Cramer, 2014, Chemical science.

Understanding the structure and dynamics of hydrogenases by ultrafast and two-dimensional infrared spectroscopy† †Electronic supplementary information (ESI) available: Supplementary figures. Description of the Morse fit. Analysis of CN stretch vibrational relaxation. References. See DOI: 10.1039/c9s

G. M. Greetham, O. Lenz, N. T. Hunt, 2019, Chemical science.

Resonance Raman spectroscopy on [NiFe] hydrogenase provides structural insights into catalytic intermediates and reactions.

O. Lenz, P. Hildebrandt, I. Zebger, 2014, Journal of the American Chemical Society.

vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an O 2-tolerant NAD +-reducing [ NiFe ] hydrogenase †

I. Zebger, S. Cramer, Yoshihito Tanaka, 2015 .

An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2 -Tolerant Hydrogenase.

M. Driess, I. Zebger, Shenglai Yao, 2017, Angewandte Chemie.