Revealing a role for the G subunit in mediating interactions between the nitrogenase component proteins

Pence, Natasha; Lewis, Nathan M.; Alleman, Alexander B.; Seefeldt, Lance C.; Peters, John W.

doi:10.1016/j.jinorgbio.2020.111273

Cited by 17 publications

(21 citation statements)

References 39 publications

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“…A notable exception in this group is the vnfDGK operon, which is expressed approximately fivefold higher in V compared with Fe-only conditions. Previous transcriptome analysis of this operon also detected significant repression under Fe-only conditions (Hamilton et al, 2011;Pence et al, 2021). This makes physiological sense since the structural subunits of the V nitrogenase are not essential for growth in V-limiting conditions when expression of the iron-only nitrogenase is activated.…”

Section: Involvement Of Vnfz In Vanadium Regulationmentioning

confidence: 82%

Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii

Appia-Ayme

Little

Chandra

et al. 2022

Molecular Microbiology

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The ability to carry out biological nitrogen fixation, a key process in the nitrogen cycle that underpins sustainable agriculture, is conferred in diverse bacteria and archaea by nitrogenase enzymes that catalyse the reduction of gaseous dinitrogen to ammonia. All diazotrophs that have been sequenced so far encode molybdenum nitrogenase with an active site co-factor designated as FeMo-co that contains a complex inorganic cluster [7Fe-9S-C-Mo] in which the molybdenum atom is bound to a molecule of R-homocitrate (Burén et al., 2020;Einsle & Rees, 2020). However, in addition to expressing the molybdenum nitrogenase enzyme, some diazotrophs also

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Section: Involvement Of Vnfz In Vanadium Regulationmentioning

confidence: 82%

Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii

Appia-Ayme

Little

Chandra

et al. 2022

Molecular Microbiology

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“…Specialized sites within the G-subunit are distal from the G-D interface. These include one residue close to the presumed Hsubunit binding site, which might contribute to a previously proposed role in mediating H-subunit binding specificity 25 .…”

Section: The G-subunit Confers Specialization Between Vnf and Anf Nit...mentioning

confidence: 94%

“…Nevertheless, nitrogenase evolution appears to have since uniquely elaborated upon this structural scheme. A striking distinction in all experimentally characterized Vnf and Anf nitrogenases is an additional, functionally enigmatic protein subunit that is not present in Nif, referred to here as the "G-subunit" [22][23][24][25] . However, the .…”

Section: Introductionmentioning

confidence: 99%

An orphan protein drove the ecological expansion of nitrogen fixation

Cuevas-Zuviría

Garcia

Carruthers

et al. 2023

Preprint

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Nitrogenases have catalyzed biological nitrogen fixation for billions of years and revolutionized planet Earth by supplying essential nitrogen to the biosphere. How these molecular machines were built and distributed by microbial processes and a shifting geochemical landscape remains an open question. Here, we probe the birth and functional evolution of the G-subunit, an integral, Precambrian component of certain nitrogenases that makes its appearance midway through the history of nitrogen fixation. Our results establish the G-subunit as an unprecedented molecular novelty that was integrated into preexisting interaction pathways for nitrogenase metallocluster incorporation. In the wake of Earth oxygenation, the G-subunit primed nitrogenases and their microbial hosts to exploit newly diversified geochemical environments. The history of the nitrogenase G-subunit showcases the elaborate tango between contingent evolutionary events and environmental conditions that together open an adaptive frontier for molecular innovations with global consequences.

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“…Putting the lo-CO VFe protein under turnover conditions (adding VnfH and ditionite) resulted in the release of CH 4 . The catalytic relevance of the isolated lo-CO state was further demonstrated by turning over 13 CO labeled lo-CO VFe protein in the presence of 12 CO, to release the partially labeled 13 CH 2 12 CH 2 product. For the first time, the hi-CO EPR signal of VnfDGK was observed after reducing CO under a decreased electron flux, by exchanging the VnfH of A. vinelandii with the VnfH of Methanosarcina acetivorans.…”

Section: Co Reduction By the V Nitrogenasementioning

confidence: 99%

“…The function of VnfG and AnfG is unknown, but an involvement in V/Fe-only nitrogenase maturation as well as Fe protein and VFe/FeFe protein complex formation and electron transfer have been suggested. [12] The Fe proteins encoded by the nifH, vnfH or anfH gene form homodimers with a subunit bridging [Fe 4 S 4 ] cluster responsible for electron delivery.…”

Section: Nitrogenases: Isozymes Structures and Mechanismmentioning

confidence: 99%

The Conversion of Carbon Monoxide and Carbon Dioxide by Nitrogenases

Oehlmann

Rebelein

2021

ChemBioChem

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Nitrogenases are the only known family of enzymes that catalyze the reduction of molecular nitrogen (N2) to ammonia (NH3). The N2 reduction drives biological nitrogen fixation and the global nitrogen cycle. Besides the conversion of N2, nitrogenases catalyze a whole range of other reductions, including the reduction of the small gaseous substrates carbon monoxide (CO) and carbon dioxide (CO2) to hydrocarbons. However, it remains an open question whether these ‘side reactivities’ play a role under environmental conditions. Nonetheless, these reactivities and particularly the formation of hydrocarbons have spurred the interest in nitrogenases for biotechnological applications. There are three different isozymes of nitrogenase: the molybdenum and the alternative vanadium and iron‐only nitrogenase. The isozymes differ in their metal content, structure, and substrate‐dependent activity, despite their homology. This minireview focuses on the conversion of CO and CO2 to methane and higher hydrocarbons and aims to specify the differences in activity between the three nitrogenase isozymes.

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Revealing a role for the G subunit in mediating interactions between the nitrogenase component proteins

Cited by 17 publications

References 39 publications

Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii

Interactions between paralogous bacterial enhancer‐binding proteins enable metal‐dependent regulation of alternative nitrogenases in Azotobacter vinelandii

An orphan protein drove the ecological expansion of nitrogen fixation

The Conversion of Carbon Monoxide and Carbon Dioxide by Nitrogenases

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