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Title: Solar powered biohydrogen production requires specific localization of the hydrogenase

Journal Article · · Energy & Environmental Science
DOI:https://doi.org/10.1039/C4EE02502D· OSTI ID:1166649
 [1];  [2];  [3];  [4];  [5];  [2];  [2];  [6];  [4];  [4]
  1. Univ. of Warwick, Coventry (United Kingdom). Systems Biology Centre
  2. Imperial College, London (United Kingdom)
  3. National Renewable Energy Lab. (NREL), Golden, CO (United States); Univ. of Colorado, Boulder, CO (United States)
  4. Queen Mary Univ. of London, London (United Kingdom)
  5. King's College London (United Kingdom)
  6. Univ. of Kiel (Germany)
+ Show Author Affiliations

Cyanobacteria contain a bidirectional [NiFe] hydrogenase which transiently produces hydrogen upon exposure of anoxic cells to light, potentially acting as a “valve” releasing excess electrons from the electron transport chain. However, its interaction with the photosynthetic electron transport chain remains unclear. By GFP-tagging the HoxF diaphorase subunit we show that the hydrogenase is thylakoid associated, comprising a population dispersed uniformly through the thylakoids and a subpopulation localized to discrete puncta in the distal thylakoid. Thylakoid localisation of both the HoxH and HoxY hydrogenase subunits is confirmed by immunogold electron microscopy. The diaphorase HoxE subunit is essential for recruitment to the dispersed thylakoid population, potentially anchoring the hydrogenase to the membrane, but aggregation to puncta occurs through a distinct HoxE-independent mechanism. Membrane association does not require NDH-1. Localization is dynamic on a scale of minutes, with anoxia and high light inducing a significant redistribution between these populations in favour of puncta. Lastly, since HoxE is essential for access to its electron donor, electron supply to the hydrogenase depends on a physiologically controlled localization, potentially offering a new avenue to enhance photosynthetic hydrogen production by exploiting localization/aggregation signals.

Research Organization:
National Renewable Energy Laboratory (NREL), Golden, CO (United States)
Sponsoring Organization:
USDOE Office of Energy Efficiency and Renewable Energy (EERE), Sustainable Transportation Office. Hydrogen Fuel Cell Technologies Office (HFTO)
Grant/Contract Number:
AC36-08-GO28308
OSTI ID:
1166649
Report Number(s):
NREL/JA-2700-60384; EESNBY; MainId:15049; UUID:43e0a336-5416-e311-a16d-d89d67143433; MainAdminID:3527
Journal Information:
Energy & Environmental Science, Vol. 7, Issue 11; ISSN 1754-5692
Publisher:
Royal Society of ChemistryCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 9 works
Citation information provided by
Web of Science

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Cited By (2)

Cyanobacterial Hydrogenases and Hydrogen Metabolism Revisited: Recent Progress and Future Prospects journal May 2015
Metalloproteins in the Biology of Heterocysts journal April 2019

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