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![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Minimal and hybrid hydrogenases are active from archaea
Chris Greening1, Princess R Cabotaje2, Luis E Valentin Alvarado3
1Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia; SAEF: Securing Antarctica's Environmental Future, Monash University, Clayton, VIC, Australia.
Anaerobic archaea possess diverse [FeFe] hydrogenases, previously thought absent in archaea. This study reveals novel hydrogenase adaptations and evolutionary links in archaeal metabolism.
Area of Science:
- Microbiology
- Biochemistry
- Evolutionary Biology
Background:
- Microbial hydrogen (H2) cycling is crucial for anoxic ecosystems.
- [FeFe] hydrogenases were historically believed to be exclusive to bacteria and eukaryotes.
Purpose of the Study:
- To investigate the presence and function of [FeFe] hydrogenases in anaerobic archaea.
- To characterize novel archaeal hydrogenase systems and their evolutionary significance.
Main Methods:
- Genomic analysis of existing and new archaeal genomes.
- Biochemical experiments to confirm enzyme activity.
- Phylogenetic analysis and structural modeling.
Main Results:
- [FeFe] hydrogenases are present in nine archaeal phyla and expressed by Asgard archaea.
- An ultraminimal hydrogenase was identified in DPANN archaea.
- Hybrid [FeFe] and [NiFe] hydrogenase complexes were discovered in ten archaeal orders.
Conclusions:
- Anaerobic archaea possess diverse and ancient [FeFe] hydrogenase lineages.
- Novel metabolic adaptations and streamlined H2 catalysts in archaea were revealed.
- A deep evolutionary history and intertwined evolution between [FeFe] and [NiFe] hydrogenases were elucidated.
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