Author

S. Shima

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 2 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

M. Gehl· 3 shared U. Demmer· 2 shared U. Ermler· 2 shared A. A. Auer· 1 shared A. N. Pravdivtsev· 1 shared C. Griesinger· 1 shared C. Riplinger· 1 shared F. Neese· 1 shared

Activity by Year

2022-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

M. Gehl

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Convergent evolution of (beta alpha)8-barrel fold methylene-tetrahydropterin reductases utilizing a common catalytic mechanism

M. Gehl, U. Demmer, U. Ermler, S. Shima

This paper identifies a common catalytic mechanism among methylene-tetrahydropterin reductases despite low sequence identity and convergent evolution.

bioRxiv · Sep 18, 2023 · PreprintBiochemistry

Sensitivity-enhanced magnetic resonance reveals hydrogen intermediates during active -hydrogenase catalysis

L. Kaltschnee, A. N. Pravdivtsev, M. Gehl, G. Huang, G. L. Stoychev, C. Riplinger, M. Keitel, F. Neese, J.-B. Hövener, A. A. Auer, C. Griesinger, S. Shima, S. Glöggler

This study uses sensitivity-enhanced magnetic resonance to identify new hydrogen species in [Fe]-hydrogenase catalysis, advancing understanding of hydrogen metabolism and catalyst design.

bioRxiv · May 10, 2023 · PreprintBiophysics

Crystal structure of FAD-independent methylene-tetrahydrofolate reductase from Mycobacterium hassiacum

M. Gehl, U. Demmer, U. Ermler, S. Shima

The paper reports the crystal structure of Mfr from M. hassiacum, showing structural similarity to MTHFR despite different catalytic mechanisms and coenzyme specificity.

bioRxiv · Nov 18, 2022Biochemistry