受强制性开放获取政策约束的文章 - Lars Lauterbach了解详情
无法在其他位置公开访问的文章：13 篇
Probing the Active Site of an O2‐Tolerant NAD+‐Reducing [NiFe]‐Hydrogenase from Ralstonia eutropha H16 by In Situ EPR and FTIR Spectroscopy
M Horch, L Lauterbach, M Saggu, P Hildebrandt, F Lendzian, R Bittl, ...
Angewandte Chemie International Edition 49 (43), 8026-8029, 2010
强制性开放获取政策： German Research Foundation
The Hydrogenase Subcomplex of the NAD+‐Reducing [NiFe] Hydrogenase from Ralstonia eutropha – Insights into Catalysis and Redox Interconversions
L Lauterbach, J Liu, M Horch, P Hummel, A Schwarze, M Haumann, ...
European Journal of Inorganic Chemistry 2011 (7), 1067-1079, 2011
强制性开放获取政策： German Research Foundation
Asymmetric Biocatalytic Amination of Ketones at the Expense of NH3 and Molecular Hydrogen
AK Holzer, K Hiebler, FG Mutti, RC Simon, L Lauterbach, O Lenz, ...
Organic letters 17 (10), 2431-2433, 2015
强制性开放获取政策： German Research Foundation, European Commission
Reversible Active Site Sulfoxygenation Can Explain the Oxygen Tolerance of a NAD+-Reducing [NiFe] Hydrogenase and Its Unusual Infrared Spectroscopic …
M Horch, L Lauterbach, MA Mroginski, P Hildebrandt, O Lenz, I Zebger
Journal of the American Chemical Society 137 (7), 2555-2564, 2015
强制性开放获取政策： German Research Foundation
Systematic evaluation of the dihydrogen-oxidising and NAD+-reducing soluble [NiFe]-hydrogenase from Ralstonia eutropha H16 as a cofactor regeneration catalyst
J Ratzka, L Lauterbach, O Lenz, MB Ansorge-Schumacher
Biocatalysis and Biotransformation 29 (6), 246-252, 2011
强制性开放获取政策： German Research Foundation
Oxygen-tolerant hydrogenases and their biotechnological potential
O Lenz, L Lauterbach, S Frielingsdorf, B Friedrich
Biohydrogen, 61-96, 2015
强制性开放获取政策： German Research Foundation
Stability enhancement of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase by a combination of immobilisation and chemical modification
N Herr, J Ratzka, L Lauterbach, O Lenz, MB Ansorge-Schumacher
Journal of Molecular Catalysis B: Enzymatic 97, 169-174, 2013
强制性开放获取政策： German Research Foundation
Stabilisation of the NAD+-reducing soluble [NiFe]-hydrogenase from Ralstonia eutropha H16 through modification with methoxy-poly (ethylene) glycol
J Ratzka, L Lauterbach, O Lenz, MB Ansorge-Schumacher
Journal of Molecular Catalysis B: Enzymatic 74 (3-4), 219-223, 2012
强制性开放获取政策： German Research Foundation
How to make the reducing power of H2 available for in vivo biosyntheses and biotransformations
L Lauterbach, O Lenz
Current opinion in chemical biology 49, 91-96, 2019
强制性开放获取政策： German Research Foundation
Impact of the Iron–Sulfur Cluster Proximal to the Active Site on the Catalytic Function of an O2-Tolerant NAD+-Reducing [NiFe]-Hydrogenase
K Karstens, S Wahlefeld, M Horch, M Grunzel, L Lauterbach, F Lendzian, ...
Biochemistry 54 (2), 389-403, 2015
强制性开放获取政策： German Research Foundation
Untersuchung des katalytischen Zentrums der O2‐toleranten NAD+‐reduzierenden [NiFe]‐Hydrogenase von Ralstonia eutropha H16 mit In‐situ‐EPR‐und‐FTIR‐Spektroskopie
M Horch, L Lauterbach, M Saggu, P Hildebrandt, F Lendzian, R Bittl, ...
Angewandte Chemie 122 (43), 8200-8203, 2010
强制性开放获取政策： German Research Foundation
Cascade biotransformation to access 3‐methylpiperidine in whole cells
N Borlinghaus, L Weinmann, F Krimpzer, PN Scheller, A Al‐Shameri, ...
ChemCatChem 11 (23), 5738-5742, 2019
强制性开放获取政策： German Research Foundation
Active Site of the NAD+-Reducing Hydrogenase from Ralstonia eutropha Studied by EPR Spectroscopy
J Löwenstein, L Lauterbach, C Teutloff, O Lenz, R Bittl
The Journal of Physical Chemistry B 119 (43), 13834-13841, 2015
强制性开放获取政策： German Research Foundation
可在其他位置公开访问的文章：34 篇
Catalytic Production of Hydrogen Peroxide and Water by Oxygen-Tolerant [NiFe]-Hydrogenase during H2 Cycling in the Presence of O2
L Lauterbach, O Lenz
Journal of the American Chemical Society 135 (47), 17897-17905, 2013
强制性开放获取政策： German Research Foundation
H2‐driven cofactor regeneration with NAD(P)+‐reducing hydrogenases
L Lauterbach, O Lenz, KA Vincent
The FEBS journal 280 (13), 3058-3068, 2013
强制性开放获取政策： German Research Foundation
A modular system for regeneration of NAD cofactors using graphite particles modified with hydrogenase and diaphorase moieties
HA Reeve, L Lauterbach, PA Ash, O Lenz, KA Vincent
Chemical Communications 48 (10), 1589-1591, 2012
强制性开放获取政策： German Research Foundation
Enzyme‐modified particles for selective biocatalytic hydrogenation by hydrogen‐driven NADH recycling
HA Reeve, L Lauterbach, O Lenz, KA Vincent
ChemCatChem 7 (21), 3480-3487, 2015
强制性开放获取政策： German Research Foundation, European Commission
Catalytic properties of the isolated diaphorase fragment of the NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha
L Lauterbach, Z Idris, KA Vincent, O Lenz
PloS one 6 (10), e25939, 2011
强制性开放获取政策： German Research Foundation
Nuclear resonance vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an O 2-tolerant NAD+-reducing [NiFe] hydrogenase
L Lauterbach, H Wang, M Horch, LB Gee, Y Yoda, Y Tanaka, I Zebger, ...
Chemical Science 6 (2), 1055-1060, 2015
强制性开放获取政策： US Department of Energy, US National Institutes of Health, German Research …
Powering artificial enzymatic cascades with electrical energy
A Al‐Shameri, MC Petrich, K Junge Puring, UP Apfel, BM Nestl, ...
Angewandte Chemie International Edition 59 (27), 10929-10933, 2020
强制性开放获取政策： German Research Foundation, Fraunhofer-Gesellschaft
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