Fundamental Electrostatics Explains Why Ferredoxin- and HiPIP-Type Proteins Favor Different Redox Transitions in [4Fe-4S]-Cys
                    4
                    Clusters

Rajeev Ranjan Roy; Maxim Janzen; G. Matthias Ullmann

doi:10.1021/acs.jpcb.6c00593

journal article Mar 27, 2026

Fundamental Electrostatics Explains Why Ferredoxin- and HiPIP-Type Proteins Favor Different Redox Transitions in [4Fe-4S]-Cys 4 Clusters

Rajeev Ranjan Roy

Maxim Janzen

G. Matthias Ullmann

The Journal of Physical Chemistry B Vol. 130 No. 14 pp. 3855-3866 · American Chemical Society (ACS)

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Details

Published: Mar 27, 2026
Vol/Issue: 130(14)
Pages: 3855-3866
License: View

Authors

R

Rajeev Ranjan Roy

Computational Biochemistry, Universitätsstr. 30, NW I; University of Bayreuth

M

Maxim Janzen

Computational Biochemistry, Universitätsstr. 30, NW I; University of Bayreuth

G

G. Matthias Ullmann

Computational Biochemistry, Universitätsstr. 30, NW I; University of Bayreuth

Funding

Deutsche Forschungsgemeinschaft Award: SPP 1927 - UL-174-9 - 311144407

Cite This Article

Rajeev Ranjan Roy, Maxim Janzen, G. Matthias Ullmann (2026). Fundamental Electrostatics Explains Why Ferredoxin- and HiPIP-Type Proteins Favor Different Redox Transitions in [4Fe-4S]-Cys 4 Clusters. The Journal of Physical Chemistry B, 130(14), 3855-3866. https://doi.org/10.1021/acs.jpcb.6c00593

Fundamental Electrostatics Explains Why Ferredoxin- and HiPIP-Type Proteins Favor Different Redox Transitions in [4Fe-4S]-Cys 4 Clusters

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