학술논문
Minimal and hybrid hydrogenases are active from archaea.
Document Type
Academic Journal
Author
Greening C; Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia; SAEF: Securing Antarctica's Environmental Future, Monash University, Clayton, VIC, Australia. Electronic address: chris.greening@monash.edu.; Cabotaje PR; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.; Valentin Alvarado LE; Department of Earth and Planetary Science, University of California, Berkeley, Berkeley, CA 94709, USA.; Leung PM; Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia; SAEF: Securing Antarctica's Environmental Future, Monash University, Clayton, VIC, Australia.; Land H; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.; Rodrigues-Oliveira T; Department of Functional and Evolutionary Ecology, Archaea Biology and Ecogenomics Unit, University of Vienna, Vienna, Austria.; Ponce-Toledo RI; Department of Functional and Evolutionary Ecology, Archaea Biology and Ecogenomics Unit, University of Vienna, Vienna, Austria.; Senger M; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.; Klamke MA; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.; Milton M; Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia.; Lappan R; Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia; SAEF: Securing Antarctica's Environmental Future, Monash University, Clayton, VIC, Australia.; Mullen S; Department of Earth and Planetary Science, University of California, Berkeley, Berkeley, CA 94709, USA.; West-Roberts J; Department of Earth and Planetary Science, University of California, Berkeley, Berkeley, CA 94709, USA.; Mao J; Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia; Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia.; Song J; Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia.; Schoelmerich M; Department of Earth and Planetary Science, University of California, Berkeley, Berkeley, CA 94709, USA.; Stairs CW; Department of Biology, Lund University, Lund, Sweden.; Schleper C; Department of Functional and Evolutionary Ecology, Archaea Biology and Ecogenomics Unit, University of Vienna, Vienna, Austria.; Grinter R; Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia. Electronic address: rhys.grinter@monash.edu.; Spang A; Department of Marine Microbiology and Biogeochemistry, Royal Netherlands Institute for Sea Research, Den Hoorn, the Netherlands; Department of Evolutionary and Population Biology, Institute for Biodiversity and Ecosystem Dynamics, University of Amsterdam, Amsterdam, the Netherlands. Electronic address: anja.spang@nioz.nl.; Banfield JF; Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia; Department of Earth and Planetary Science, University of California, Berkeley, Berkeley, CA 94709, USA. Electronic address: jbanfield@berkeley.edu.; Berggren G; Department of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden. Electronic address: gustav.berggren@kemi.uu.se.
Source
Publisher: Cell Press Country of Publication: United States NLM ID: 0413066 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1097-4172 (Electronic) Linking ISSN: 00928674 NLM ISO Abbreviation: Cell Subsets: MEDLINE
Subject
Language
English
Abstract
Microbial hydrogen (H 2 ) cycling underpins the diversity and functionality of diverse anoxic ecosystems. Among the three evolutionarily distinct hydrogenase superfamilies responsible, [FeFe] hydrogenases were thought to be restricted to bacteria and eukaryotes. Here, we show that anaerobic archaea encode diverse, active, and ancient lineages of [FeFe] hydrogenases through combining analysis of existing and new genomes with extensive biochemical experiments. [FeFe] hydrogenases are encoded by genomes of nine archaeal phyla and expressed by H 2 -producing Asgard archaeon cultures. We report an ultraminimal hydrogenase in DPANN archaea that binds the catalytic H-cluster and produces H 2 . Moreover, we identify and characterize remarkable hybrid complexes formed through the fusion of [FeFe] and [NiFe] hydrogenases in ten other archaeal orders. Phylogenetic analysis and structural modeling suggest a deep evolutionary history of hybrid hydrogenases. These findings reveal new metabolic adaptations of archaea, streamlined H 2 catalysts for biotechnological development, and a surprisingly intertwined evolutionary history between the two major H 2 -metabolizing enzymes.
Competing Interests: Declaration of interests J.F.B. is a co-founder of Metagenomi. A patent on this discovery and application of ultraminimal hydrogenases was submitted.
(Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
Competing Interests: Declaration of interests J.F.B. is a co-founder of Metagenomi. A patent on this discovery and application of ultraminimal hydrogenases was submitted.
(Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)