Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer

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Science  18 Jan 2019:
Vol. 363, Issue 6424, pp. 257-260
DOI: 10.1126/science.aau3613

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Plugging into the pump

Photosynthetic organisms use light to fix carbon dioxide in a process that requires both chemical reducing equivalents and adenosine triphosphate (ATP). Balancing the ratio of these inputs is accomplished by a short circuit in electron flow through photosynthetic complex I, a proton pump that contributes to ATP production but does not increase net reducing equivalents in the cell. Schuller et al. solved a cryo–electron microscopy structure of photosynthetic complex I (see the Perspective by Brandt) and went on to reconstitute electron transfer using the electron carrier protein ferredoxin.

Science, this issue p. 257; see also p. 230


Photosynthetic complex I enables cyclic electron flow around photosystem I, a regulatory mechanism for photosynthetic energy conversion. We report a 3.3-angstrom-resolution cryo–electron microscopy structure of photosynthetic complex I from the cyanobacterium Thermosynechococcus elongatus. The model reveals structural adaptations that facilitate binding and electron transfer from the photosynthetic electron carrier ferredoxin. By mimicking cyclic electron flow with isolated components in vitro, we demonstrate that ferredoxin directly mediates electron transfer between photosystem I and complex I, instead of using intermediates such as NADPH (the reduced form of nicotinamide adenine dinucleotide phosphate). A large rate constant for association of ferredoxin to complex I indicates efficient recognition, with the protein subunit NdhS being the key component in this process.

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