Protein–Protein Interaction Regulates the Direction of Catalysis and Electron Transfer in a Redox Enzyme Complex
Protein-protein complexes are fundamental to life where they are key to processes ranging from central metabolism to cell signaling. Transient protein-protein interactions generally underpin the electron-transfer (ET) pathways of respiration.1 One of the many well-characterized examples of a transient ET complex is that between cytochrome c and cytochrome c oxidase.2-5 The interaction between these partner proteins is weak and dynamic. This ensures the frequent exchange of partner proteins as required to support electron flux in cases where the sole function of one of the proteins is to shuttle electrons between redox partners.1 While it is generally assumed that such transient protein-protein interactions are specific, for Paracoccus denitrificans it has recently been shown that seven proteins in a respiratory network interact in a seemingly ill-defined manner. This results in an intricate electron-transfer network that may be better suited to successful colonization of habitats with changing resources.
- Research Organization:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 1089064
- Report Number(s):
- PNNL-SA-96978; KP1702030
- Journal Information:
- Journal of the American Chemical Society, Vol. 135, Issue 28; ISSN 0002-7863
- Publisher:
- American Chemical Society (ACS)
- Country of Publication:
- United States
- Language:
- English
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