Abstract
Te self-assembly of enzyme proteins on 2D nanomaterials has enabled the construction and functional control of viable biochemical pathways. However, enzymatic cascades, which combine essential components of the photosynthetic and respiratory electron transport chains in tandem, have thus-far remained elusive. Herein, we have investigated a galvanic biohybrid nano system coupling photosystem I and cytochrome c oxidase on the surface of graphene oxide nanosheets in colloidal suspension. Te oriented immobilization of the enzymes was facilitated by Ni-coordination sites tethered to the carbon basal plane, with negligible parasitic O2 consumption. Transient absorption and electrochemical measurements provided evidence of electron transfer between donors and acceptors, leading to light-induced O2 consumption of up to 70 out of 120 O2 molecules/s/CcO unit. Graphene oxide behaves as an electronic reservoir and as an electroactive support, enabling electron transport, in concert with cytochrome c, as well as small-molecule redox mediators and reductants. This study provides a state-of-the-art approach for the exploration of photoelectron transfer in membrane-free suspensions of nano surface-anchored photosynthetic–respiratory enzymatic chains.
Recommended Citation
X. Zhu and M. J. Kummer and C. E. Lubner and V. Kurashov and W. Carr and J. H. Golbeck and R. A. Niederman and L. G. Mourokh and S. D. Minteer and P. G. Falkowski and M. Vittadello, "A Photosynthetic–respiratory Electron Transport Chain Chimera Based on Photosystem I and Cytochrome C Oxidase on Graphene Oxide," Proceedings of the National Academy of Sciences of the United States of America, vol. 123, no. 7, article no. e2524884123, National Academy of Sciences, Feb 2026.
The definitive version is available at https://doi.org/10.1073/pnas.2524884123
Department(s)
Chemistry
Publication Status
Open Access
Keywords and Phrases
cytochrome c oxidase; electron transfer; graphene oxide; | oxygen-reduction reaction; photosystem I
International Standard Serial Number (ISSN)
1091-6490; 0027-8424
Document Type
Article - Journal
Document Version
Final Version
File Type
text
Language(s)
English
Rights
© 2026 The Authors, All rights reserved.
Creative Commons Licensing
This work is licensed under a Creative Commons Attribution 4.0 License.
Publication Date
17 Feb 2026
PubMed ID
41665998
Comments
Université Pierre et Marie Curie, Grant FA9550-16-1-0279