Christian Teutloff
Overview
Explore the profile of Christian Teutloff including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
48
Citations
419
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Gerland L, Diehl A, Erdmann N, Hiller M, Lang C, Teutloff C, et al.
Chemistry
. 2024 Nov;
31(2):e202402454.
PMID: 39541567
Phytochromes perceive subtle changes in the light environment and convert them into biological signals by photoconversion between the red-light absorbing (Pr) and the far-red-absorbing (Pfr) states. In the primitive bacteriophytochromes...
2.
Perez-Bitrian A, Munarriz J, Krause K, Schlogl J, Hoffmann K, Sturm J, et al.
Chem Sci
. 2024 Apr;
15(15):5564-5572.
PMID: 38638238
Compounds containing Mn-O bonds are of utmost importance in biological systems and catalytic processes. Nevertheless, mononuclear manganese complexes containing all O-donor ligands are still rare. Taking advantage of the low...
3.
Xu J, Pan S, Yao S, Lorent C, Teutloff C, Zhang Z, et al.
J Am Chem Soc
. 2024 Feb;
146(9):6025-6036.
PMID: 38408197
The formation of isolable monatomic Bi complexes and Bi radical species is challenging due to the pronounced reducing nature of metallic bismuth. Here, we report a convenient strategy to tame...
4.
Duffus B, Gauglitz M, Teutloff C, Leimkuhler S
J Inorg Biochem
. 2024 Feb;
253:112487.
PMID: 38306887
Metal-dependent, nicotine adenine dinucleotide (NAD)-dependent formate dehydrogenases (FDHs) are complex metalloenzymes coupling biochemical transformations through intricate electron transfer pathways. Rhodobacter capsulatus FDH is a model enzyme for understanding coupled catalysis,...
5.
Schmidt A, Kalms J, Lorent C, Katz S, Frielingsdorf S, Evans R, et al.
Chem Sci
. 2023 Oct;
14(40):11105-11120.
PMID: 37860641
The membrane-bound [NiFe]-hydrogenase of is a rare example of a truly O-tolerant hydrogenase. It catalyzes the oxidation of H into 2e and 2H in the presence of high O concentrations....
6.
Salsi F, Wang S, Teutloff C, Busse M, Neville M, Hagenbach A, et al.
Angew Chem Int Ed Engl
. 2023 Mar;
62(19):e202300254.
PMID: 36855012
The first consistent series of mononuclear 17-electron complexes of three Group 7 elements has been isolated in crystalline form and studied by X-ray diffraction and spectroscopic methods. The paramagnetic compounds...
7.
Kielb P, Teutloff C, Bittl R, Gray H, Winkler J
J Phys Chem B
. 2022 Oct;
126(40):7943-7949.
PMID: 36191240
We have investigated the roles of tyrosine (Tyr) and tryptophan (Trp) residues in the four-electron reduction of oxygen catalyzed by laccase (SLAC). During normal enzymatic turnover in laccases, reducing equivalents...
8.
Intraligand Charge Transfer Enables Visible-Light-Mediated Nickel-Catalyzed Cross-Coupling Reactions
Cavedon C, Gisbertz S, Reischauer S, Vogl S, Sperlich E, Burke J, et al.
Angew Chem Int Ed Engl
. 2022 Sep;
61(46):e202211433.
PMID: 36161982
We demonstrate that several visible-light-mediated carbon-heteroatom cross-coupling reactions can be carried out using a photoactive Ni precatalyst that forms in situ from a nickel salt and a bipyridine ligand decorated...
9.
Kulka-Peschke C, Schulz A, Lorent C, Rippers Y, Wahlefeld S, Preissler J, et al.
J Am Chem Soc
. 2022 Sep;
144(37):17022-17032.
PMID: 36084022
NAD-reducing [NiFe] hydrogenases are valuable biocatalysts for H-based energy conversion and the regeneration of nucleotide cofactors. While most hydrogenases are sensitive toward O and elevated temperatures, the soluble NAD-reducing [NiFe]...
10.
Jeoung J, Fesseler J, Domnik L, Klemke F, Sinnreich M, Teutloff C, et al.
Angew Chem Int Ed Engl
. 2022 Feb;
61(18):e202117000.
PMID: 35133707
Ni,Fe-containing carbon monoxide dehydrogenases (CODHs) catalyze the reversible reduction of CO to CO. Several anaerobic microorganisms encode multiple CODHs in their genome, of which some, despite being annotated as CODHs,...