What does this research mean for the field?

The HoxEFU subcomplex of the HOX [NiFe]-hydrogenase forms a dimer, and its electron transfer kinetics for NADH oxidation can be accurately modeled using inter-cofactor distances and determined Em values to reproduce observed equilibrium populations of reduced cofactors. Novelty: ClaimNovelty.INCREMENTAL. Consensus alignment: ConsensusAlignment.NEUTRAL.

What question did this study set out to answer?

To elucidate the quaternary structure and determine the electron transfer kinetics of the HoxEFU subcomplex from the Synechocystis sp. PCC 6803 HOX [NiFe]-hydrogenase.

September 2, 2026Cell Reports Physical ScienceOpen Access

Cryo-EM map and functional electron transport studies of the HoxEFU subcomplex of the HOX NiFe-hydrogenase from Synechocystis sp. PCC 6803

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Authors

MDMichael E. Dawson EKEffie C. Kisgeropoulos JGJosephine N. Gruber

Discussion

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Overview

Structural and spectroscopic analysis uncovers electron transfer kinetics within the cyanobacterial HoxEFU hydrogenase subcomplex, highlighting mechanisms coordinating NADH and ferredoxin redox...

Key Points

To elucidate the quaternary structure and determine the electron transfer kinetics of the HoxEFU subcomplex from the Synechocystis sp. PCC 6803 HOX [NiFe]-hydrogenase.
Generated a low-resolution single-particle cryo-electron microscopy (cryo-EM) map of resting-state HoxEFU.
Predicted the dimeric complex using AlphaFold to determine inter-cofactor distances.
Measured cofactor reduction potentials (Em) and performed electron paramagnetic resonance (EPR) spectroscopy to simulate electron transfer rate constants (kET) during NADH oxidation.
Cryo-EM map dimensions of the resting-state HoxEFU subcomplex accommodated a dimeric assembly of HoxEFU monomers.
Kinetic modeling based on calculated rate constants successfully reproduced the equilibrium populations of reduced cofactors observed via EPR spectroscopy during NADH oxidation.

Cite This Study

Dawson et al. (2026) studied this question.

synapsesocial.com/papers/6a97e2eac562ede874ec74a0 https://doi.org/10.1016/j.xcrp.2026.103513

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September 2, 2026Cell Reports Physical ScienceOpen Access

Cryo-EM map and functional electron transport studies of the HoxEFU subcomplex of the HOX NiFe-hydrogenase from Synechocystis sp. PCC 6803

View Full Paper

Ask AI

Bookmark

Authors

MDMichael E. Dawson EKEffie C. Kisgeropoulos JGJosephine N. Gruber

Discussion

Member takes

Overview

Structural and spectroscopic analysis uncovers electron transfer kinetics within the cyanobacterial HoxEFU hydrogenase subcomplex, highlighting mechanisms coordinating NADH and ferredoxin redox...

Key Points

To elucidate the quaternary structure and determine the electron transfer kinetics of the HoxEFU subcomplex from the Synechocystis sp. PCC 6803 HOX [NiFe]-hydrogenase.
Generated a low-resolution single-particle cryo-electron microscopy (cryo-EM) map of resting-state HoxEFU.
Predicted the dimeric complex using AlphaFold to determine inter-cofactor distances.
Measured cofactor reduction potentials (Em) and performed electron paramagnetic resonance (EPR) spectroscopy to simulate electron transfer rate constants (kET) during NADH oxidation.
Cryo-EM map dimensions of the resting-state HoxEFU subcomplex accommodated a dimeric assembly of HoxEFU monomers.
Kinetic modeling based on calculated rate constants successfully reproduced the equilibrium populations of reduced cofactors observed via EPR spectroscopy during NADH oxidation.

Cite This Study

Dawson et al. (2026) studied this question.

synapsesocial.com/papers/6a97e2eac562ede874ec74a0 https://doi.org/10.1016/j.xcrp.2026.103513

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