Publications by authors named "Alexander B Alleman"

The availability of fixed nitrogen is a limiting factor in the net primary production of all ecosystems. Diazotrophs overcome this limit through the conversion of atmospheric dinitrogen to ammonia. Diazotrophs are phylogenetically diverse bacteria and archaea that exhibit a wide range of lifestyles and metabolisms, including obligate anaerobes and aerobes that generate energy through heterotrophic or autotrophic metabolisms.

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Biological nitrogen fixation requires large amounts of energy in the form of ATP and low potential electrons to overcome the high activation barrier for cleavage of the dinitrogen triple bond. The model aerobic nitrogen-fixing bacteria, Azotobacter vinelandii, generates low potential electrons in the form of reduced ferredoxin (Fd) and flavodoxin (Fld) using two distinct mechanisms via the enzyme complexes Rnf and Fix. Both Rnf and Fix are expressed during nitrogen fixation, but deleting either or genes has little effect on diazotrophic growth.

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Article Synopsis
  • The study highlights the potential of biological nitrogen fixation (BNF) to reduce reliance on chemical fertilizers, but emphasizes existing knowledge gaps about the process.
  • A metabolic model of the nitrogen-fixing bacterium Azotobacter vinelandii shows it uses respiration mechanisms to manage oxygen levels while sustaining energy needs for BNF.
  • The research indicates that understanding the bacterium’s energy balance is crucial for future agricultural engineering efforts, especially in addressing global fertilizer accessibility issues.
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Azotobacter vinelandii contains three forms of nitrogenase known as the Mo-, V-, and Fe-nitrogenases. They are all two-component enzyme systems, where the catalytic component, referred to as NifDK, VnfDGK, and AnfDGK, associates with the reductase component, the Fe protein or NifH, VnfH, and AnfH respectively. AnfDGK and VnfDGK have an additional subunit compared to NifDK, termed gamma or AnfG and VnfG, whose role is unknown.

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Alkenes and ketones are two classes of ubiquitous, toxic organic compounds in natural environments produced in several biological and anthropogenic processes. In spite of their toxicity, these compounds are utilized as primary carbon and energy sources or are generated as intermediate metabolites in the metabolism of other compounds by many diverse bacteria. The aerobic metabolism of some of the smallest and most volatile of these compounds (propylene, acetone, isopropanol) involves novel carboxylation reactions resulting in a common product acetoacetate.

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Most biological nitrogen fixation (BNF) results from the activity of the molybdenum nitrogenase (Mo-nitrogenase, Nif), an oxygen-sensitive metalloenzyme complex found in all known diazotrophs. Two alternative forms of nitrogenase, the vanadium nitrogenase (V-nitrogenase, Vnf) and the iron-only nitrogenase (Fe-only nitrogenase, Anf) have also been identified in the genome of some organisms that encode for Nif. It has been suggested that alternative nitrogenases were responsible for N2-fixation on early Earth because oceans were depleted of bioavailable Mo.

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Article Synopsis
  • Microorganisms use carboxylase enzymes to create carbon-carbon bonds by incorporating CO2 or bicarbonate into specific molecules.
  • Acetone carboxylases (ACs) convert acetone and bicarbonate into acetoacetate and utilize ATP for substrate activation, without relying on organic cofactors like biotin.
  • The study reveals the structural mechanisms behind AC's function, showing how it undergoes significant changes during the catalytic process to efficiently convert CO into biomass, which is important for the global carbon cycle.
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