What is he best known for?
The fields of study he is best known for:
Stereochemistry, Biochemistry, Nitrogenase, Active site and Cytochrome c are his primary areas of study.
His Stereochemistry research includes elements of Oxidoreductase, Catalytic cycle, Reaction intermediate and Binding site.
His Biochemistry research focuses on subjects like Bacteria, which are linked to Transporter and Ammonium.
His Nitrogenase study incorporates themes from Crystallography, Crystal structure and Cofactor.
The concepts of his Active site study are interwoven with issues in Metalloprotein, Molecule and Sirtuin.
His Cytochrome c study incorporates themes from Periplasmic space, Cytochrome, Nitrite reductase and Signal peptide.
His most cited work include:
- Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor. (732 citations)
- Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor. (732 citations)
- Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor (509 citations)
What are the main themes of his work throughout his whole career to date?
Oliver Einsle mainly focuses on Biochemistry, Stereochemistry, Nitrogenase, Crystallography and Active site.
As a member of one scientific family, Oliver Einsle mostly works in the field of Biochemistry, focusing on Nitrite and, on occasion, Formate.
His research on Stereochemistry also deals with topics like
- Heme which is related to area like Cytochrome,
- Nitrous-oxide reductase that intertwine with fields like Pseudomonas stutzeri and Inorganic chemistry.
Much of his study explores Nitrogenase relationship to Cofactor.
The various areas that Oliver Einsle examines in his Crystallography study include Aquifex aeolicus, Dimer and Azurin.
His Cytochrome c nitrite reductase research integrates issues from Reductase and Hydroxylamine.
He most often published in these fields:
- Biochemistry (40.37%)
- Stereochemistry (31.19%)
- Nitrogenase (21.10%)
What were the highlights of his more recent work (between 2015-2021)?
- Stereochemistry (31.19%)
- Nitrogenase (21.10%)
- Biochemistry (40.37%)
In recent papers he was focusing on the following fields of study:
The scientist’s investigation covers issues in Stereochemistry, Nitrogenase, Biochemistry, Cofactor and Active site.
The Stereochemistry study combines topics in areas such as Transferase, Nitrous-oxide reductase, Organic chemistry, Reductive elimination and Binding site.
His Nitrogenase research includes elements of Triple bond, Catalysis, Molybdenum and Metalloprotein.
His biological study spans a wide range of topics, including Crystallography, FeMoco, Vanadium and Vanadium nitrogenase.
In his study, Enzyme catalysis is strongly linked to Nitrogen fixation, which falls under the umbrella field of Biochemistry.
In his research on the topic of Cofactor, Bioinorganic chemistry, Topology and Molecule is strongly related with Combinatorial chemistry.
Between 2015 and 2021, his most popular works were:
- Anaerobic Microbial Degradation of Hydrocarbons : from Enzymatic Reactions to the Environment (126 citations)
- The structure of vanadium nitrogenase reveals an unusual bridging ligand (101 citations)
- A bound reaction intermediate sheds light on the mechanism of nitrogenase (88 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Stereochemistry, Biochemistry, Nitrogenase, Cofactor and Molybdenum.
His Stereochemistry research is multidisciplinary, incorporating perspectives in Transferase, Acetylation, BRD4, Substrate and Organic chemistry.
His studies in Nitrogenase integrate themes in fields like Reductive elimination and Active site.
His Cofactor study which covers Reaction intermediate that intersects with Triple bond.
His Molybdenum study combines topics in areas such as FeMoco and Vanadium.
His FeMoco research includes themes of Crystallography, Ion, Oxidation state and Azotobacter vinelandii.
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