Ivan Voloshyn
PhD student at Department of Chemistry for Life Sciences; Biochemistry; Senger Group
- E-mail:
- ivan.voloshyn@kemi.uu.se
- Visiting address:
- Husargatan 3
752 37 Uppsala - Postal address:
- Box 576
75123 Uppsala
- ORCID:
- 0009-0004-1518-0232
Keywords
- protein purification
- protein crystallography
- enzyme catalysis

Publications
Recent publications
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Part of Analytical Chemistry, p. 26393-26403, 2025
- DOI for Reconsidering the Enzyme Kinetics of [FeFe]-Hydrogenases: Improved Turnover Rates and New Insights into pH and Potential Dependence with Eu(II)-Based Solution Assays
- Download full text (pdf) of Reconsidering the Enzyme Kinetics of [FeFe]-Hydrogenases: Improved Turnover Rates and New Insights into pH and Potential Dependence with Eu(II)-Based Solution Assays
-
Secondary structure changes as the potential H2 sensing mechanism of group D [FeFe]-hydrogenases
Part of Chemical Communications, p. 10914-10917, 2024
- DOI for Secondary structure changes as the potential H2 sensing mechanism of group D [FeFe]-hydrogenases
- Download full text (pdf) of Secondary structure changes as the potential H2 sensing mechanism of group D [FeFe]-hydrogenases
-
Structural photoactivation of a bathy phytochrome resolved by time-resolved X-ray crystallography
All publications
Articles in journal
-
Part of Analytical Chemistry, p. 26393-26403, 2025
- DOI for Reconsidering the Enzyme Kinetics of [FeFe]-Hydrogenases: Improved Turnover Rates and New Insights into pH and Potential Dependence with Eu(II)-Based Solution Assays
- Download full text (pdf) of Reconsidering the Enzyme Kinetics of [FeFe]-Hydrogenases: Improved Turnover Rates and New Insights into pH and Potential Dependence with Eu(II)-Based Solution Assays
-
Secondary structure changes as the potential H2 sensing mechanism of group D [FeFe]-hydrogenases
Part of Chemical Communications, p. 10914-10917, 2024
- DOI for Secondary structure changes as the potential H2 sensing mechanism of group D [FeFe]-hydrogenases
- Download full text (pdf) of Secondary structure changes as the potential H2 sensing mechanism of group D [FeFe]-hydrogenases