Publications by authors named "Paul R F Cordero"

The NAD-reducing soluble [NiFe] hydrogenase (SH) is the key enzyme for production and consumption of molecular hydrogen (H) in Synechocystis sp. PCC6803. In this study, we focused on the reductase module of the SynSH and investigated the structural and functional aspects of its subunits, particularly the so far elusive role of HoxE.

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Despite the increasing demand for efficient and sustainable chemical processes, the development of scalable systems using biocatalysis for fine chemical production remains a significant challenge. We have developed a scalable flow system using immobilized enzymes to facilitate flavin-dependent biocatalysis, targeting as a proof-of-concept asymmetric alkene reduction. The system integrates a flavin-dependent Old Yellow Enzyme (OYE) and a soluble hydrogenase to enable H-driven regeneration of the OYE cofactor FMNH.

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Article Synopsis
  • Carbon monoxide (CO) is known for its dangerous toxicity, particularly affecting proteins like respiratory terminal oxidases in bacteria, but its antibacterial effects are still debated.
  • The study investigates the resistance of mycobacteria to CO, finding only minor growth inhibition and highlighting the role of cytochrome oxidase, which shows resistance to CO, while adjacent complexes are affected negatively.
  • Overall, mycobacteria demonstrate a strong ability to adapt to CO presence with minimal proteome changes, mainly through utilizing CO-resistant respiratory mechanisms.
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F is a low-potential redox cofactor used by diverse bacteria and archaea. In mycobacteria, this cofactor has multiple roles, including adaptation to redox stress, cell wall biosynthesis, and activation of the clinical antitubercular prodrugs pretomanid and delamanid. A recent biochemical study proposed a revised biosynthesis pathway for F in mycobacteria; it was suggested that phosphoenolpyruvate served as a metabolic precursor for this pathway, rather than 2-phospholactate as long proposed, but these findings were subsequently challenged.

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Article Synopsis
  • * The study identifies two iron-sulfur cluster proteins, HucE and HhyE, that are essential for hydrogen consumption in these bacteria; deleting their genes significantly hinders hydrogen oxidation and reduces bacterial growth.
  • * The researchers hypothesize that these proteins facilitate electron transfer between hydrogenases and the respiratory chain, highlighting their importance for atmospheric hydrogen oxidation and the need for further investigation into their functions.
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Article Synopsis
  • Aerobic soil bacteria can survive in nutrient-poor conditions by metabolizing atmospheric hydrogen (H), which plays a crucial role in the global H cycle and aids microbial productivity in oligotrophic environments.
  • The soil bacterium has two types of [NiFe] hydrogenases, Huc and Hhy, that although they seem similar, are expressed and function differently during various growth phases, with Huc active during early growth stages and Hhy utilized for long-term survival.
  • Huc and Hhy are integrated into the aerobic respiratory chain and interact differently with respiratory processes; Huc aids in energy conservation during initial growth, while Hhy supports energy needs during carbon limitation.
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Carbon monoxide (CO) is a ubiquitous atmospheric trace gas produced by natural and anthropogenic sources. Some aerobic bacteria can oxidize atmospheric CO and, collectively, they account for the net loss of ~250 teragrams of CO from the atmosphere each year. However, the physiological role, genetic basis, and ecological distribution of this process remain incompletely resolved.

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Most aerobic bacteria exist in dormant states within natural environments. In these states, they endure adverse environmental conditions such as nutrient starvation by decreasing metabolic expenditure and using alternative energy sources. In this study, we investigated the energy sources that support persistence of two aerobic thermophilic strains of the environmentally widespread but understudied phylum Chloroflexi.

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