Interplay between hydrogen production and photosynthesis in a green alga expressing an active photosystem I-hydrogenase chimera. (22nd June 2022)

• Record Type: Journal Article
• Authors: Kanygin, Andrey; Smith, Alec; Nagy, Valéria; Tóth, Szilvia Z.; Redding, Kevin E.
• Is Part Of: International journal of hydrogen energy. Volume 47:Number 52(2022)
• Page Start: 21969
• Page End: 21983
• Publication Date: 2022-06-22
• Subjects: Biohydrogen -- Hydrogenase -- Photosystem I -- Chlamydomonas -- Green alga -- Photosynthesis; ATP adenosine triphosphate -- ADP adenosine diphosphate -- CAM chloramphenicol -- CBB Calvin–Benson–Bassham -- Chl chlorophyll -- DBMIB dibromothymoquinone -- β-DDM n-dodecyl-β-D-maltoside -- DCMU 3-(3, 4-dichlorophenyl)-1, 1-dimethylurea -- EDTA ethylenediamine tetraacetate -- Fd ferredoxin -- FNR Fd-NADP+ reductase -- GA glycolaldehyde -- LEF linear electron flow -- MIMS membrane inlet mass spectrometry -- MV methyl viologen -- NADP nicotinamide adenine dinucleotide phosphate -- PAR photosynthetically active radiation -- PCR polymerase chain reaction -- PS photosystem -- RMVA reduced methyl viologen assay -- SUF sulfur utilization factor -- TAP Tris acetate phosphate -- TBP Tris bicarbonate phosphate. SUF; Hydrogen as fuel -- Periodicals; Hydrogène (Combustible) -- Périodiques; Hydrogen as fuel; Periodicals; 665.81
• DOI: 10.1016/j.ijhydene.2022.03.096
• Languages: English
• ISSNs: 0360-3199

Abstract

Abstract: We have previously created and expressed a chimeric polypeptide joining the PsaC subunit of Photosystem I (PSI) to the HydA2 hydrogenase of Chlamydomonas reinhardtii and demonstrated that it assembles into the PSI complex and feeds electrons directly to the hydrogenase domain, allowing for prolonged photobiological hydrogen production. Here we describe a new PSI-hydrogenase chimera using HydA1, the more abundant and physiologically active endogenous hydrogenase of this alga. When the PsaC-HydA1 polypeptide was expressed in a C. reinhardtii strain lacking endogenous hydrogenases, it was assembled into active PSI-HydA1 complexes that were accumulated at a level ∼75% that of PSI, which is ∼5 times higher than the PSI-HydA2 chimera. Hydrogen production by the chimera could be restored after complete inactivation by oxygen without requiring new synthesis of PSI or the PsaC-HydA1 polypeptide, demonstrating that the complex could be repaired in vivo . The PSI-HydA1 chimera reduces ferredoxin in vivo to such an extent that it can drive the Calvin-Benson-Bassham cycle, leading to high O2 production rates, and eventually resulting in inactivation of the hydrogenase; use of media that drastically diminished CO2 fixation and an O2 -scavenging material allowed H2 production for at least 4 days. Highlights: The PsaC-HydA1 fusion is expressed and assembles on photosystem I in vivo . The chimeric PSI-HydA1 complex is accumulated at levels approaching wild-type PSI. Light-dependent H2 evolution switches to H2 uptake upon CO2 fixation. PsaC-HydA1 can be reactivated in vivo after O2 inactivation.