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The Diviner Lunar Radiometer Experiment on the Lunar Reconnaissance Orbiter (LRO) has been mapping the surface temperatures of the Moon since 5 July 2009. Diviner has since collected over 500 billion radiometric measurements with excellent spatial and local time coverage. However, the most recently published high-resolution Diviner global maps only use data collected from 2009 to 2016. In this work, we compile ∼13 years of Diviner data to produce improved global maps of nighttime brightness temperature, bolometric temperature, regolith temperature, and rock abundance (RA). Errors in Diviner's pointing have been corrected and past effective field of view modeling has been optimized to improve data georeferencing without spatial interpolation. We estimate an effective resolution of ∼330 m longitudinally and ∼700 m latitudinally at the equator, which corresponds to an improvement of ∼3.5× longitudinally and ∼1.3× latitudinally. In addition, we develop a thermal model that accounts for indirect scattering and emission from surrounding topography. The resulting temperature anomaly maps better highlight variations in temperature caused by thermophysical properties by removing most topographic effects. These improvements allow for the identification of smaller and fainter thermal features than was previously possible. The improved effective resolution of Diviner maps allows for excellent spatial correlation with other high-resolution data sets. To demonstrate this, we compare Diviner RA to a manual survey of boulders in the Apollo 17 landing site region. We show that Diviner RA correlates well with the areal fraction of rocks larger than ∼1–2 m in diameter visible in LRO Camera imagery.

Both Earth and the Moon share a common history regarding the epoch of large basin formation, though only the lunar geologic record preserves any appreciable record of this Late Heavy Bombardment. The emergence of Earth's first life is approximately contemporaneous with the Late Heavy Bombardment; understanding the latter informs the environmental conditions of the former, which are likely necessary to constrain the mechanisms of abiogenesis. While the relative formation time of most of the Moon's large basins is known, the absolute timing is not. The timing of Crisium Basin's formation is one of many important events that must be constrained and would require identifying and dating impact melt formed in the Crisium event. To inform a future lunar sample dating mission, we thus characterized possible outcrops of impact melt. We determined that several mare lava-embayed kipukas could contain impact melt, though the rim and central peaks of the partially lava-flooded Yerkes Crater likely contain the most pure and intact Crisium impact melt. It is here where future robotic and/or human missions could confidently add a key missing piece to the puzzle of the combined issues of early Earth-Moon bombardment and the emergence of life., (©2019. The Authors.)

We find that the reflectance of the lunar surface within 5 ° of latitude of the South Pole increases rapidly with decreasing temperature, near ~110K, behavior consistent with the presence of surface water iceThe North polar region does not show this behavior, nor do South polar surfaces at latitudes more than 5° from the pole. This South pole reflectance anomaly persists when analysis is limited to surfaces with slopes less than 10° to eliminate false detection due to the brightening effect of mass wasting, and also when the very bright south polar crater Shackleton is excluded from the analysis. We also find that south polar regions of permanent shadow that have been reported to be generally brighter at 1064 nm do not show anomalous reflectance when their annual maximum surface temperatures are too high to preserve water ice. This distinction is not observed at the North Pole. The reflectance excursion on surfaces with maximum temperatures below 110K is superimposed on a general trend of increasing reflectance with decreasing maximum temperature that is present throughout the polar regions in the north and south; we attribute this trend to a temperature or illumination-dependent space weathering effect (e.g. Hemingway et al. 2015). We also find a sudden increase in reflectance with decreasing temperature superimposed on the general trend at 200K and possibly at 300K. This may indicate the presence of other volatiles such as sulfur or organics. We identified and mapped surfaces with reflectances so high as to be unlikely to be part of an ice-free population. In this south we find a similar distribution found by Hayne et al. 2015 based on UV properties. In the north a cluster of pixels near that pole may represent a limited frost exposure.

Lunar swirls are high-albedo markings on the Moon that occur in both mare and highland terrains; their origin remains a point of contention. Here, we use data from the Lunar Reconnaissance Orbiter Diviner Lunar Radiometer to support the hypothesis that the swirls are formed as a result of deflection of the solar wind by local magnetic fields. Thermal infrared data from this instrument display an anomaly in the position of the silicate Christiansen Feature consistent with reduced space weathering. These data also show that swirl regions are not thermophysically anomalous, which strongly constrains their formation mechanism. The results of this study indicate that either solar wind sputtering and implantation are more important than micrometeoroid bombardment in the space-weathering process, or that micrometeoroid bombardment is a necessary but not sufficient process in space weathering, which occurs on airless bodies throughout the solar system.

One of the key problems in determining lunar surface composition for thermal-infrared measurements is the lack of comparable laboratory-measured spectra. As the surface is typically composed of fine-grained particulates, the lunar environment induces a thermal gradient within the near sub-surface, altering the emission spectra: this environment must therefore be simulated in the laboratory, considerably increasing the complexity of the measurement. Previous measurements have created this thermal gradient by either heating the cup in which the sample sits or by illuminating the sample using a solar-like source. This is the first setup able to measure in both configurations, allowing direct comparisons to be made between the two. Also, measurements across a wider spectral range and at a much higher spectral resolution can be acquired using this new setup. These are required to support new measurements made by the Diviner Lunar Radiometer, the first multi-spectral thermal-infrared instrument to orbit the Moon. Results from the two different heating methods are presented, with measurements of a fine-grained quartz sample compared to previous similar measurements, plus measurements of a common lunar highland material, anorthite. The results show that quartz gives the same results for both methods of heating, as predicted by previous studies, though the anorthite spectra are different. The new calibration pipeline required to convert the raw data into emissivity spectra is described also.

Diviner Lunar Radiometer Experiment surface-temperature maps reveal the existence of widespread surface and near-surface cryogenic regions that extend beyond the boundaries of persistent shadow. The Lunar Crater Observation and Sensing Satellite (LCROSS) struck one of the coldest of these regions, where subsurface temperatures are estimated to be 38 kelvin. Large areas of the lunar polar regions are currently cold enough to cold-trap water ice as well as a range of both more volatile and less volatile species. The diverse mixture of water and high-volatility compounds detected in the LCROSS ejecta plume is strong evidence for the impact delivery and cold-trapping of volatiles derived from primitive outer solar system bodies.

The Lunar Reconnaissance Orbiter (LRO) Diviner instrument detected a thermal emission signature 90 seconds after the Lunar Crater Observation and Sensing Satellite (LCROSS) Centaur impact and on two subsequent orbits. The impact heated a region of 30 to 200 square meters to at least 950 kelvin, providing a sustained heat source for the sublimation of up to ~300 kilograms of water ice during the 4 minutes of LCROSS post-impact observations. Diviner visible observations constrain the mass of the sunlit ejecta column to be ~10(-6) to 10(-5) kilograms per square meter, which is consistent with LCROSS estimates used to derive the relative abundance of the ice within the regolith.

Using data from the Diviner Lunar Radiometer Experiment, we show that four regions of the Moon previously described as "red spots" exhibit mid-infrared spectra best explained by quartz, silica-rich glass, or alkali feldspar. These lithologies are consistent with evolved rocks similar to lunar granites in the Apollo samples. The spectral character of these spots is distinct from surrounding mare and highlands material and from regions composed of pure plagioclase feldspar. The variety of landforms associated with the silicic spectral character suggests that both extrusive and intrusive silicic magmatism occurred on the Moon. Basaltic underplating is the preferred mechanism for silicic magma generation, leading to the formation of extrusive landforms. This mechanism or silicate liquid immiscibility could lead to the formation of intrusive bodies.

We obtained direct global measurements of the lunar surface using multispectral thermal emission mapping with the Lunar Reconnaissance Orbiter Diviner Lunar Radiometer Experiment. Most lunar terrains have spectral signatures that are consistent with known lunar anorthosite and basalt compositions. However, the data have also revealed the presence of highly evolved, silica-rich lunar soils in kilometer-scale and larger exposures, expanded the compositional range of the anorthosites that dominate the lunar crust, and shown that pristine lunar mantle is not exposed at the lunar surface at the kilometer scale. Together, these observations provide compelling evidence that the Moon is a complex body that has experienced a diverse set of igneous processes.

Throughout molecular evolution, organisms create assorted chemicals in response to varying ecological niches. Catalytic landscapes underlie metabolic evolution, wherein mutational steps alter the biosynthetic properties of enzymes. Here we report the first systematic quantitative characterization of the catalytic landscape underlying the evolution of sesquiterpene chemical diversity. On the basis of our previous discovery of a set of nine naturally occurring amino acid substitutions that functionally interconverted orthologous sesquiterpene synthases from Nicotiana tabacum and Hyoscyamus muticus, we created a library of all possible residue combinations (2(9) = 512) in the N. tabacum enzyme. The product spectra of 418 active enzymes revealed a rugged landscape where several minimal combinations of the nine mutations encode convergent solutions to the interconversions of parental activities. Quantitative comparisons indicated context dependence for mutational effects--epistasis--in product specificity and promiscuity. These results provide a measure of the mutational accessibility of phenotypic variability in a diverging lineage of terpene synthases.

The human pathogen Pseudomonas aeruginosa produces pyocyanin, a blue-pigmented phenazine derivative, which is known to play a role in virulence. Pyocyanin is produced from chorismic acid via the phenazine pathway, nine proteins encoded by a gene cluster. Phenazine-1-carboxylic acid, the initial phenazine formed, is converted to pyocyanin in two steps that are catalyzed by the enzymes PhzM and PhzS. PhzM is an adenosylmethionine dependent methyltransferase, and PhzS is a flavin dependent hydroxylase. It has been shown that PhzM is only active in the physical presence of PhzS, suggesting that a protein-protein interaction is involved in pyocyanin formation. Such a complex would prevent the release of 5-methyl-phenazine-1-carboxylate, the putative intermediate, and an apparently unstable compound. Here, we describe the three-dimensional structure of PhzS, solved by single anomalous dispersion, at a resolution of 2.4 A. The structure reveals that PhzS is a member of the family of aromatic hydroxylases characterized by p-hydroxybenzoate hydroxylase. The flavin cofactor of PhzS is in the solvent exposed out orientation typically seen in unliganded aromatic hydroxylases. The PhzS flavin, however, appears to be held in a strained conformation by a combination of stacking interactions and hydrogen bonds. The structure suggests that access to the active site is gained via a tunnel on the opposite side of the protein from where the flavin is exposed. The C-terminal 23 residues are disordered as no electron density is present for these atoms. The probable location of the C-terminus, near the substrate access tunnel, suggests that it may be involved in substrate binding as has been shown for another structural homologue, RebC. This region also may be an element of a PhzM-PhzS interface. Aromatic hydroxylases have been shown to catalyze electrophilic substitution reactions on activated substrates. The putative PhzS substrate, however, is electron deficient and unlikely to act as a nucleophile, suggesting that PhzS may use a different mechanism than its structural relatives.

Solavetivone, a potent antifungal phytoalexin, is derived from a vetispirane-type sesquiterpene, premnaspirodiene, by a putative regio- and stereo-specific hydroxylation, followed by a second oxidation to yield the alpha,beta-unsaturated ketone. Mechanistically, these reactions could occur via a single, multifunctional cytochrome P450 or some combination of cytochrome P450s and a dehydrogenase. We report here the characterization of a single cytochrome P450 enzyme, Hyoscyamus muticus premnaspirodiene oxygenase (HPO), that catalyzes these successive reactions at carbon 2 (C-2) of the spirane substrate. HPO also catalyzes the equivalent regio-specific (C-2) hydroxylation of several eremophilane-type (decalin ring system) sesquiterpenes, such as with 5-epi-aristolochene. Moreover, HPO displays interesting comparisons to other sesquiterpene hydroxylases. 5-Epi-aristolochene di-hydroxylase (EAH) differs catalytically from HPO by introducing hydroxyl groups first at C-1, then C-3 of 5-epi-aristolochene. HPO and EAH also differ from one another by 91-amino acid differences, with four of these differences mapping to putative substrate recognition regions 5 and 6. These four positions were mutagenized alone and in various combinations in both HPO and EAH and the mutant enzymes were characterized for changes in substrate selectivity, reaction product specificity, and kinetic properties. These mutations did not alter the regio- or stereo-specificity of either HPO or EAH, but specific combinations of the mutations did improve the catalytic efficiencies 10-15-fold. Molecular models and comparisons between HPO and EAH provide insights into the catalytic properties of these enzymes of specialized metabolism in plants.

Terpenes are structurally diverse compounds that are of interest because of their biological activities and industrial value. These compounds consist of chirally rich hydrocarbon backbones derived from terpene synthases, which are subsequently decorated with hydroxyl substituents catalyzed by terpene hydroxylases. Availability of these compounds is, however, limited by intractable synthetic means and because they are produced in low amounts and as complex mixtures by natural sources. We engineered yeast for sesquiterpene accumulation by introducing genetic modifications that enable the yeast to accumulate high levels of the key intermediate farnesyl diphosphate (FPP). Co-expression of terpene synthase genes diverted the enlarged FPP pool to greater than 80 mg/L of sesquiterpene. Efficient coupling of terpene production with hydroxylation was also demonstrated by coordinate expression of terpene hydroxylase activity, yielding 50 mg/L each of hydrocarbon and hydroxylated products. These yeast now provide a convenient format for investigating catalytic coupling between terpene synthases and hydroxylases, as well as a platform for the industrial production of high value, single-entity and stereochemically unique terpenes., ((c) 2006 Wiley Periodicals, Inc.)

Pyocyanin is a biologically active phenazine produced by the human pathogen Pseudomonas aeruginosa. It is thought to endow P. aeruginosa with a competitive growth advantage in colonized tissue and is also thought to be a virulence factor in diseases such as cystic fibrosis and AIDS where patients are commonly infected by pathogenic Pseudomonads due to their immunocompromised state. Pyocyanin is also a chemically interesting compound due to its unusual oxidation-reduction activity. Phenazine-1-carboxylic acid, the precursor to the bioactive phenazines, is synthesized from chorismic acid by enzymes encoded in a seven-gene cistron in P. aeruginosa and in other Pseudomonads. Phenzine-1-carboxylic acid is believed to be converted to pyocyanin by the sequential actions of the putative S-adenosylmethionine-dependent N-methyltransferase PhzM and the putative flavin-dependent hydroxylase PhzS. Here we report the 1.8 A crystal structure of PhzM determined by single anomalous dispersion. Unlike many methyltransferases, PhzM is a dimer in solution. The 36 kDa PhzM polypeptide folds into three domains. The C-terminal domain exhibits the alpha/beta-hydrolase fold typical of small molecule methyltransferases. Two smaller N-terminal domains form much of the dimer interface. Structural alignments with known methyltransferases show that PhzM is most similar to the plant O-methyltransferases that are characterized by an unusual intertwined dimer interface. The structure of PhzM contains no ligands, and the active site is open and solvent-exposed when compared to structures of similar enzymes. In vitro experiments using purified PhzM alone demonstrate that it has little or no ability to methylate phenzine-1-carboxylic acid. However, when the putative hydroxylase PhzS is included, pyocyanin is readily produced. This observation suggests that a mechanism has evolved in P. aeruginosa that ensures efficient production of pyocyanin via the prevention of the formation and release of an unstable and potentially deleterious intermediate.

Terpene synthases are a mechanistically intriguing family of enzymes that catalyze complex, multistep reactions that are capable of generating hundreds of structurally diverse hydrocarbon and oxygenated scaffolds of biological and commercial importance. Interestingly, distantly related terpene synthases from fungi to plants all contain an invariant three-dimensional fold, and molecular comparisons of their active sites indicate that they are enriched with relatively inert amino acid residues that do not react directly with the reaction intermediates. Therefore, catalytic specificity appears to rely on the contour and dynamics of the active site created by the positioning of amino acid backbones and side chains on this catalytic surface and by supporting layers of residues surrounding the synthase active site cavity. Despite the high degree of structural relatedness among terpene synthases, previous studies suggest that no clear relationship between phylogenic organization and catalytic specificities is easily deciphered. We now report on the reciprocal interconversion of catalytic specificities between two distinct yet evolutionarily related terpene synthases based on the systematic identification and mutational replacement of variable residues within and surrounding the active site. Furthermore, we uncover previously undocumented biosynthetic activity during the interconversion, activity that could have been present in a common ancestor of these two highly related synthases. These results provide a simplified means for mapping structural features that are responsible for functional attributes and a strategy for identifying residues that differentiate divergent biosynthetic properties in phylogenetically related terpene synthases.

A method for the recovery of full-length cDNAs from predicted terpene synthase genes containing introns is described. The approach utilizes Agrobacterium-mediated transient expression coupled with a reverse transcription-polydeoxyribonucleotide chain reaction assay to facilitate expression cloning of processed transcripts. Subsequent expression of intronless cDNAs in a suitable prokaryotic host provides for direct functional testing of the encoded gene product. The method was optimized by examining the expression of an intron-containing beta-glucuronidase gene agroinfiltrated into petunia (Petunia hybrida) leaves, and its utility was demonstrated by defining the function of two previously uncharacterized terpene synthases. A tobacco (Nicotiana tabacum) terpene synthase-like gene containing six predicted introns was characterized as having 5-epi-aristolochene synthase activity, while an Arabidopsis (Arabidopsis thaliana) gene previously annotated as a terpene synthase was shown to possess a novel sesquiterpene synthase activity for alpha-barbatene, thujopsene, and beta-chamigrene biosynthesis.

The final step of capsidiol biosynthesis is catalyzed by 5-epiaristolochene dihydroxylase (EAH), a cytochrome P450 enzyme that catalyzes the regio- and stereospecific insertion of two hydroxyl moieties into the bicyclic sesquiterpene 5-epiaristolochene (EA). Detailed kinetic studies using EA and the two possible monohydroxylated intermediates demonstrated the release of 1beta-hydroxy-EA ((OH)EA) at high EA concentrations and a 10-fold catalytic preference for 1beta(OH)EA versus 3alpha(OH)EA, indicative of a preferred reaction order of hydroxylation at C-1, followed by that at C-3. Sequence alignments and homology modeling identified active-site residues tested for their contribution to substrate specificity and overall enzymatic activity. Mutants EAH-S368C and EAH-S368V exhibited wild-type catalytic efficiencies for 1beta(OH)EA biosynthesis, but were devoid of the successive hydroxylation activity for capsidiol biosynthesis. In contrast to EAH-S368C, EAH-S368V catalyzed the relative equal biosynthesis of 1beta(OH)EA, 2beta(OH)EA, and 3beta(OH)EA from EA with wild-type efficiency. Moreover, EAH-S368V converted approximately 1.5% of these monohydroxylated products to their respective ketone forms. Alanine and threonine mutations at position 368 were significantly compromised in their conversion rates of EA to capsidiol and correlated with 3.6- and 5.7-fold increases in their Km values for the 1beta(OH)EA intermediate, respectively. A role for Ile486 in the successive hydroxylations of EA was also suggested by the EAH-I468A mutant, which produced significant amounts 1beta(OH)EA, but negligible amounts of capsidiol from EA. The altered product profile of the EAH-I486A mutant correlated with a 3.6-fold higher Km for EA and a 4.4-fold slower turnover rate (kcat) for 1beta(OH)EA. These kinetic and mutational studies were correlated with substrate docking predictions to suggest how Ser368 and Ile486 might contribute to active-site topology, substrate binding, and substrate presentation to the oxo-Fe-heme reaction center.