Molecular evolution of gas cavity in [NiFeSe] hydrogenases resurrected in silico.
Ontology highlight
ABSTRACT:
SUBMITTER: Tamura T
PROVIDER: S-EPMC4730141 | biostudies-literature | 2016 Jan
REPOSITORIES: biostudies-literature
Similar Datasets
Project description:Hydrogenases are efficient biocatalysts for H2 production and oxidation with various potential biotechnological applications.[NiFe]-class hydrogenases are highly active in both production and oxidation processes-albeit primarily biased to the latter-but suffer from being sensitive to O2.[NiFeSe] hydrogenases are a subclass of [NiFe] hydrogenases with, usually, an increased insensitivity to aerobic environments. In this study we aim to understand the structural causes of the low sensitivity of a [NiFeSe]-hydrogenase, when compared with a [NiFe] class enzyme, by studying the diffusion of O2. To unravel the differences between the two enzymes, we used computational methods comprising Molecular Dynamics simulations with explicit O2 and Implicit Ligand Sampling methodologies. With the latter, we were able to map the free energy landscapes for O2 permeation in both enzymes. We derived pathways from these energy landscapes and selected the kinetically more relevant ones with reactive flux analysis using transition path theory. These studies evidence the existence of quite different pathways in both enzymes and predict a lower permeation efficiency for O2 in the case of the [NiFeSe]-hydrogenase when compared with the [NiFe] enzyme. These differences can explain the experimentally observed lower inhibition by O2 on [NiFeSe]-hydrogenases, when compared with [NiFe]-hydrogenases. A comprehensive map of the residues lining the most important O2 pathways in both enzymes is also presented.
| S-EPMC7324405 | biostudies-literature
Project description:Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions of the iron-sulfur-containing catalytic site with the local protein environment are thought to contribute to differences in catalytic reactivity, but this has not been demonstrated. The microbe Clostridium pasteurianum produces three [FeFe]-hydrogenases that differ in "catalytic bias" by exerting a disproportionate rate acceleration in one direction or the other that spans a remarkable 6 orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicates that protein secondary interactions directly influence the relative stabilization/destabilization of different oxidation states of the active site metal cluster. This selective stabilization or destabilization of oxidation states can preferentially promote hydrogen oxidation or proton reduction and represents a simple yet elegant model by which a protein catalytic site can confer catalytic bias.
| S-EPMC8653774 | biostudies-literature
Project description:Molecular hydrogen (H2) has been suggested to be a beneficial treatment for a range of species, from humans to plants. Hydrogenases catalyze the reversible oxidation of H2, and are found in many organisms, including plants. One of the cellular effects of H2 is the selective removal of reactive oxygen species (ROS) and reactive nitrogen species (RNS), specifically hydroxyl radicals and peroxynitrite. Therefore, the function of hydrogenases and the action of H2 needs to be reviewed in the context of the signalling roles of a range of redox active compounds. Enzymes can be controlled by the covalent modification of thiol groups, and although motifs targeted by nitric oxide (NO) can be predicted in hydrogenases sequences it is likely that the metal prosthetic groups are the target of inhibition. Here, a selection of hydrogenases, and the possibility of their control by molecules involved in redox signalling are investigated using a bioinformatics approach. Methods of treating plants with H2 along with the role of H2 in plants is also briefly reviewed. It is clear that studies report significant effects of H2 on plants, improving growth and stress responses, and therefore future work needs to focus on the molecular mechanisms involved.
| S-EPMC7569912 | biostudies-literature
Project description:There is growing evidence of rapid genetic adaptation of natural populations to environmental change, opening the perspective that evolutionary trait change may subsequently impact ecological processes such as population dynamics, community composition, and ecosystem functioning. To study such eco-evolutionary feedbacks in natural populations, however, requires samples across time. Here, we capitalize on a resurrection ecology study that documented rapid and adaptive evolution in a natural population of the water flea Daphnia magna in response to strong changes in predation pressure by fish, and carry out a follow-up mesocosm experiment to test whether the observed genetic changes influence population dynamics and top-down control of phytoplankton. We inoculated populations of the water flea D. magna derived from three time periods of the same natural population known to have genetically adapted to changes in predation pressure in replicate mesocosms and monitored both Daphnia population densities and phytoplankton biomass in the presence and absence of fish. Our results revealed differences in population dynamics and top-down control of algae between mesocosms harboring populations from the time period before, during, and after a peak in fish predation pressure caused by human fish stocking. The differences, however, deviated from our a priori expectations. An S-map approach on time series revealed that the interactions between adults and juveniles strongly impacted the dynamics of populations and their top-down control on algae in the mesocosms, and that the strength of these interactions was modulated by rapid evolution as it occurred in nature. Our study provides an example of an evolutionary response that fundamentally alters the processes structuring population dynamics and impacts ecosystem features.
| S-EPMC5748522 | biostudies-literature
Project description:A dinuclear synthetic model of the [NiFeSe] hydrogenase active site and a structural, spectroscopic and electrochemical analysis of this complex is reported. [NiFe('S2Se2')(CO)3] (H2'S2Se2' = 1,2-bis(2-thiabutyl-3,3-dimethyl-4-selenol)benzene) has been synthesized by reacting the nickel selenolate complex [Ni('S2Se2')] with [Fe(CO)3bda] (bda = benzylideneacetone). X-ray crystal structure analysis confirms that [NiFe('S2Se2')(CO)3] mimics the key structural features of the enzyme active site, including a doubly bridged heterobimetallic nickel and iron center with a selenolate terminally coordinated to the nickel center. Comparison of [NiFe('S2Se2')(CO)3] with the previously reported thiolate analogue [NiFe('S4')(CO)3] (H2'S4' = H2xbsms = 1,2-bis(4-mercapto-3,3-dimethyl-2-thiabutyl)benzene) showed that the selenolate groups in [NiFe('S2Se2')(CO)3] give lower carbonyl stretching frequencies in the IR spectrum. Electrochemical studies of [NiFe('S2Se2')(CO)3] and [NiFe('S4')(CO)3] demonstrated that both complexes do not operate as homogenous H2 evolution catalysts, but are precursors to a solid deposit on an electrode surface for H2 evolution catalysis in organic and aqueous solution.
| S-EPMC4510704 | biostudies-literature
Project description:We study the permeation dynamics of helium and carbon dioxide through an atomistically detailed model of a polymer of intrinsic microporosity, PIM-1, via non-equilibrium molecular dynamics (NEMD) simulations. This work presents the first explicit molecular modeling of gas permeation through a high free-volume polymer sample, and it demonstrates how permeability and solubility can be obtained coherently from a single simulation. Solubilities in particular can be obtained to a very high degree of confidence and within experimental inaccuracies. Furthermore, the simulations make it possible to obtain very specific information on the diffusion dynamics of penetrant molecules and yield detailed maps of gas occupancy, which are akin to a digital tomographic scan of the polymer network. In addition to determining permeability and solubility directly from NEMD simulations, the results shed light on the permeation mechanism of the penetrant gases, suggesting that the relative openness of the microporous topology promotes the anomalous diffusion of penetrant gases, which entails a deviation from the pore hopping mechanism usually observed in gas diffusion in polymers.
| S-EPMC4384093 | biostudies-literature
Project description:Following the abolishment of dual nomenclature, Stilbospora is recognised as having priority over Prosthecium. The type species of Stilbospora, S. macrosperma, is the correct name for P. ellipsosporum, the type species of Prosthecium. The closely related genus Stegonsporium is maintained as distinct from Stilbospora based on molecular phylogeny, morphology and host range. Stilbospora longicornuta and S. orientalis are described as new species from Carpinus betulus and C. orientalis, respectively. They differ from the closely related Stilbospora macrosperma, which also occurs on Carpinus, by longer, tapering gelatinous ascospore appendages and by distinct LSU, ITS rDNA, rpb2 and tef1 sequences. The asexual morphs of Stilbospora macrosperma, S.longicornuta and S. orientalis are morphologically indistinguishable; the connection to their sexual morphs is demonstrated by morphology and DNA sequences of single spore cultures derived from both ascospores and conidia. Both morphs of the three Stilbospora species on Carpinus are described and illustrated. Other species previously recognised in Prosthecium, specifically P.acerophilum, P. galeatum and P. opalus, are determined to belong to and are formally transferred to Stegonsporium. Isolates previously recognised as Stegonsporium pyriforme (syn. Prosthecium pyriforme) are determined to consist of three phylogenetically distinct lineages by rpb2 and tef1 sequence data, two of which are described as new species (S. protopyriforme, S. pseudopyriforme). Stegonsporium pyriforme is lectotypified and this species and Stilbospora macrosperma are epitypified. Based on DNA sequence data, the North American Stegonsporium acerophilum is recorded from Europe for the first time, and new hosts from Acer sect. Acer are reported for S. opalus and S. pyriforme. Stilbospora and Stegonsporium are classified within the revived family Stilbosporaceae. Prosthecium appendiculatum, P. auctum and P. innesii are shown to be unrelated to the Stilbosporaceae and are recognised in three distinct genera, Phaeodiaporthe appendiculata, Alnecium auctum n. gen. and Calosporella innesii within Diaporthaceae, Gnomoniaceae and Sydowiellaceae, respectively. The generic types of these three monotypic genera are briefly described, illustrated and lecto- and epitypfied.
| S-EPMC4312938 | biostudies-literature
Project description:In silico analysis of group 4 [NiFe]-hydrogenases from a hyperthermophilic archaeon, Thermococcus onnurineus NA1, revealed a novel tripartite gene cluster consisting of dehydrogenase-hydrogenase-cation/proton antiporter subunits, which may be classified as the new subgroup 4b of [NiFe]-hydrogenases-based on sequence motifs.
| S-EPMC2937479 | biostudies-literature
Project description:Coupling between molecules and vacuum photon fields inside an optical cavity has proven to be an effective way to engineer molecular properties, in particular reactivity. To ease the rationalization of cavity induced effects we introduce an ab initio method leading to the first fully consistent molecular orbital theory for quantum electrodynamics environments. Our framework is non-perturbative and explains modifications of the electronic structure due to the interaction with the photon field. In this work, we show that the newly developed orbital theory can be used to predict cavity induced modifications of molecular reactivity and pinpoint classes of systems with significant cavity effects. We also investigate electronic cavity-induced modifications of reaction mechanisms in vibrational strong coupling regimes.
| S-EPMC8924263 | biostudies-literature
Project description:Artificial metalloenzymes result from anchoring a metal cofactor within a host protein. Such hybrid catalysts combine the selectivity and specificity of enzymes with the versatility of (abiotic) transition metals to catalyze new-to-nature reactions in an evolvable scaffold. With the aim of improving the localization of an arylsulfonamide-bearing iridium-pianostool catalyst within human carbonic anhydrase II (hCAII) for the enantioselective reduction of prochiral imines, we introduced a covalent linkage between the host and the guest. Herein, we show that a judiciously positioned cysteine residue reacts with a p-nitropicolinamide ligand bound to iridium to afford an additional sulfonamide covalent linkage. Three rounds of directed evolution, performed on the dually anchored cofactor, led to improved activity and selectivity for the enantioselective reduction of harmaline (up to 97% ee (R) and >350 turnovers on a preparative scale). To evaluate the substrate scope, the best hits of each generation were tested with eight substrates. X-ray analysis, carried out at various stages of the evolutionary trajectory, was used to scrutinize (i) the nature of the covalent linkage between the cofactor and the host as well as (ii) the remodeling of the substrate-binding pocket.
| S-EPMC8620556 | biostudies-literature