Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPOR Article Swipe
R. P. KASHYAP
,
Natalie Walsh
,
Jaigeeth Deveryshetty
,
Monika Tokmina‐Lukaszewska
,
Kehan Zhao
,
Yunqiao J. Gan
,
Brian M. Hoffman
,
Ritimukta Sarangi
,
Brian Bothner
,
Brian Bennett
,
Edwin Antony
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1038/s41467-025-59158-7
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1038/s41467-025-59158-7
Enzymes that catalyze long-range electron transfer (ET) reactions often function as higher order complexes that possess two structurally symmetrical halves. The functional advantages for such an architecture remain a mystery. Using cryoelectron microscopy we capture snapshots of the nitrogenase-like dark-operative protochlorophyllide oxidoreductase (DPOR) during substrate binding and turnover. DPOR catalyzes reduction of the C17 = C18 double bond in protochlorophyllide during the dark chlorophyll biosynthetic pathway. DPOR is composed of electron donor (L-protein) and acceptor (NB-protein) component proteins that transiently form a complex in the presence of ATP to facilitate ET. NB-protein is an α2β2 heterotetramer with two structurally identical halves. However, our structures reveal that NB-protein becomes functionally asymmetric upon substrate binding. Asymmetry results in allosteric inhibition of L-protein engagement and ET in one half. Residues that form a conduit for ET are aligned in one half while misaligned in the other. An ATP hydrolysis-coupled conformational switch is triggered once ET is accomplished in one half. These structural changes are then relayed to the other half through a di-nuclear copper center at the tetrameric interface of the NB-protein and leads to activation of ET and substrate reduction. These findings provide a mechanistic blueprint for regulation of long-range electron transfer reactions.
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- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s41467-025-59158-7
- https://www.nature.com/articles/s41467-025-59158-7.pdf
- OA Status
- gold
- Cited By
- 1
- References
- 60
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4409736011
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Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4409736011Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1038/s41467-025-59158-7Digital Object Identifier
- Title
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Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPORWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
-
2025Year of publication
- Publication date
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2025-04-24Full publication date if available
- Authors
-
R. P. KASHYAP, Natalie Walsh, Jaigeeth Deveryshetty, Monika Tokmina‐Lukaszewska, Kehan Zhao, Yunqiao J. Gan, Brian M. Hoffman, Ritimukta Sarangi, Brian Bothner, Brian Bennett, Edwin AntonyList of authors in order
- Landing page
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https://doi.org/10.1038/s41467-025-59158-7Publisher landing page
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https://www.nature.com/articles/s41467-025-59158-7.pdfDirect link to full text PDF
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YesWhether a free full text is available
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goldOpen access status per OpenAlex
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https://www.nature.com/articles/s41467-025-59158-7.pdfDirect OA link when available
- Concepts
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Copper, Electron, Electron transfer, Materials science, Chemistry, Physics, Metallurgy, Photochemistry, Nuclear physicsTop concepts (fields/topics) attached by OpenAlex
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1Total citation count in OpenAlex
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2025: 1Per-year citation counts (last 5 years)
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60Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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