Abstract
H2 producing micro-algae such as Chlamydomonas reinhardtii (C. reinhardtii), express the strictly anaerobic enzyme FeFe-hydrogenase (HydA). In this study, we examined whether superoxide dismutase (SOD), an antioxidant, can protect HydA under aerobic conditions. We conducted in-vitro assays using purified enzymes, to analyze the activity of HydA in the presence or absence of SOD. We observed that SOD enhances HydA activity both in the presence and absence of oxygen, showing that the SOD effect on HydA activity is not strictly oxygen dependent. Furthermore, we found that SOD boosts Ferredoxin-NADP+-oxidoreductase (FNR) NDAP+ reduction but not NADPH oxidation i.e. diaphorase activity. Thus, suggesting a mechanism involving proton transfer rather than electron transfer. Based on these findings, we constructed a HydA-SOD fusion protein that further boosted hydrogen production by HydA. The HydA-SOD photosynthetic activity was enhanced by 300%, reaching 700 μmol H2 (mg [chl] hr)−1, which is the fastest photosynthetic rate ever reported for an algal HydA.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
