Formate hydrogenlyase

Finney, Alexander J.; Sargent, Frank

doi:10.1016/bs.ampbs.2019.02.004

Cited by 24 publications

(11 citation statements)

References 57 publications

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“…Transcription of ORFs by "Ca. Atribacteria" with similarity to enzymes known to be involved in electron bifurcation that results in production of molecular hydrogen included the beta subunit of the heterodisulfide reductase, formate hydrogen lyase (63), gamma subunit of the NiFe hydrogenase (64), and subunit alpha of the reversible formate dehydrogenase (65). The formate hydrogen lyase complex combines NiFe hydrogenase and soluble formate dehydrogenase to couple formate and/or CO-dependent hydrogen production to the generation of the Na ϩ motive force to generate ATP.…”

Section: Resultsmentioning

confidence: 99%

Atribacteria Reproducing over Millions of Years in the Atlantic Abyssal Subseafloor

Vuillemin

Vargas

Coskun

et al. 2020

mBio

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How microbial metabolism is translated into cellular reproduction under energy-limited settings below the seafloor over long timescales is poorly understood. Here, we show that microbial abundance increases an order of magnitude over a 5 million-year-long sequence in anoxic subseafloor clay of the abyssal North Atlantic Ocean. This increase in biomass correlated with an increased number of transcribed protein-encoding genes that included those involved in cytokinesis, demonstrating that active microbial reproduction outpaces cell death in these ancient sediments. Metagenomes, metatranscriptomes, and 16S rRNA gene sequencing all show that the actively reproducing community was dominated by the candidate phylum “Candidatus Atribacteria,” which exhibited patterns of gene expression consistent with fermentative, and potentially acetogenic, metabolism. “Ca. Atribacteria” dominated throughout the 8 million-year-old cored sequence, despite the detection limit for gene expression being reached in 5 million-year-old sediments. The subseafloor reproducing “Ca. Atribacteria” also expressed genes encoding a bacterial microcompartment that has potential to assist in secondary fermentation by recycling aldehydes and, thereby, harness additional power to reduce ferredoxin and NAD+. Expression of genes encoding the Rnf complex for generation of chemiosmotic ATP synthesis were also detected from the subseafloor “Ca. Atribacteria,” as well as the Wood-Ljungdahl pathway that could potentially have an anabolic or catabolic function. The correlation of this metabolism with cytokinesis gene expression and a net increase in biomass over the million-year-old sampled interval indicates that the “Ca. Atribacteria” can perform the necessary catabolic and anabolic functions necessary for cellular reproduction, even under energy limitation in millions-of-years-old anoxic sediments. IMPORTANCE The deep subseafloor sedimentary biosphere is one of the largest ecosystems on Earth, where microbes subsist under energy-limited conditions over long timescales. It remains poorly understood how mechanisms of microbial metabolism promote increased fitness in these settings. We discovered that the candidate bacterial phylum “Candidatus Atribacteria” dominated a deep-sea subseafloor ecosystem, where it exhibited increased transcription of genes associated with acetogenic fermentation and reproduction in million-year-old sediment. We attribute its improved fitness after burial in the seabed to its capabilities to derive energy from increasingly oxidized metabolites via a bacterial microcompartment and utilize a potentially reversible Wood-Ljungdahl pathway to help meet anabolic and catabolic requirements for growth. Our findings show that “Ca. Atribacteria” can perform all the necessary catabolic and anabolic functions necessary for cellular reproduction, even under energy limitation in anoxic sediments that are millions of years old.

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Section: Resultsmentioning

confidence: 99%

Atribacteria Reproducing over Millions of Years in the Atlantic Abyssal Subseafloor

Vuillemin

Vargas

Coskun

et al. 2020

mBio

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“…FHL complexes are biological machines for HCO 2 – /H 2 interconversion. 11 They are either membrane-associated complexes composed of a multisubunit [NiFe]-H 2 ase coupled to an FDH, 11−13 or smaller soluble complexes of an [FeFe]-H 2 ase and an FDH. 14,15 The E. coli FHL-1 complex, composed of the membrane-bound [NiFe]-H 2 ase 3 (HYD-3/HycE) and FDH-H (FdhF; Figure 1a), represents a well-studied FHL, evolving H 2 under fermentative conditions.…”

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confidence: 99%

“…14,15 The E. coli FHL-1 complex, composed of the membrane-bound [NiFe]-H 2 ase 3 (HYD-3/HycE) and FDH-H (FdhF; Figure 1a), represents a well-studied FHL, evolving H 2 under fermentative conditions. 11,12 The constituent enzymatic units of FHL-1 have been demonstrated to be reversible electrocatalysts, 16−20 but the complex is catalytically biased toward H 2 production from formate. 14,15,19 Interconversion of HCO 2 – /H 2 has also been reported in whole-cell studies, 14,20 notably in sulfate-reducing bacteria in the absence of sulfate.…”

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confidence: 99%

“…FHL complexes are biological machines for HCO 2 – /H 2 interconversion . They are either membrane-associated complexes composed of a multisubunit [NiFe]-H 2 ase coupled to an FDH, − or smaller soluble complexes of an [FeFe]-H 2 ase and an FDH. , The E. coli FHL-1 complex, composed of the membrane-bound [NiFe]-H 2 ase 3 (HYD-3/HycE) and FDH-H (FdhF; Figure a), represents a well-studied FHL, evolving H 2 under fermentative conditions. , The constituent enzymatic units of FHL-1 have been demonstrated to be reversible electrocatalysts, − but the complex is catalytically biased toward H 2 production from formate. ,, Interconversion of HCO 2 – /H 2 has also been reported in whole-cell studies, , notably in sulfate-reducing bacteria in the absence of sulfate. , Desulfovibrio vulgaris Hildenborough can grow by converting formate to H 2 , with formate oxidation catalyzed by a periplasmic FDH, and H 2 produced either via direct (periplasmic H 2 ase) or transmembrane electron transfer (cytoplasmic H 2 ase) …”

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confidence: 99%

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Reversible and Selective Interconversion of Hydrogen and Carbon Dioxide into Formate by a Semiartificial Formate Hydrogenlyase Mimic

et al. 2019

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The biological formate hydrogenlyase (FHL) complex links a formate dehydrogenase (FDH) to a hydrogenase (H2ase) and produces H2 and CO2 from formate via mixed-acid fermentation in Escherichia coli. Here, we describe an electrochemical and a colloidal semiartificial FHL system that consists of an FDH and a H2ase immobilized on conductive indium tin oxide (ITO) as an electron relay. These in vitro systems benefit from the efficient wiring of a highly active enzyme pair and allow for the reversible conversion of formate to H2 and CO2 under ambient temperature and pressure. The hybrid systems provide a template for the design of synthetic catalysts and surpass the FHL complex in vivo by storing and releasing H2 on demand by interconverting CO2/H2 and formate with minimal bias in either direction.

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“…of reductant on Earth. 97 It has not (yet) been chemically veried whether, from the iron-sulfur clusters very likely present in the "prebiotic" world, chemical accesses to catalytically active clusters mixed with other metals did exist.…”

Section: A Proposalmentioning

confidence: 99%