Application of the Electrically Scanning Microwave Radiometer (ESMR) to classification of the moisture condition of the ground

The ability of the Nimbus 5 ESMR to characterize the moisture condition of the uppermost portion of the soil was evaluated. In the absence of snow cover, ESMR-5 brightness temperatures were compared with computed upper soil zone moisture values from a soil moisture budgeting scheme. The study was conducted over the U.S. Great Plains for the late summer and early fall in 1974 and 1975. Favorable results were limited by the relatively high vegetative cover and infrequent substantial rainfalls at that time of year. Satisfactory characterization of the general moisture condition was deemed feasible in agricultural regions at times of the year when fields were nearly bare. An additional evaluation demonstrated that ESMR-6 data could delineate the active boundary of a snow pack

Application of the Nimbus 5 ESMR to rainfall detection over land surfaces

The ability of the Nimbus 5 Electrically Scanning Microwave Radiometer (ESMR) to detect rainfall over land surfaces was evaluated. The ESMR brightness temperatures (Tb sub B) were compared with rainfall reports from climatological stations for a limited number of rain events over portions of the U.S. The greatly varying emissivity of land surfaces precludes detection of actively raining areas. Theoretical calculations using a ten-layer atmospheric model showed this to be an expected result. Detection of rain which had fallen was deemed feasible over certain types of land surfaces by comparing the Tb sub B fields before and after the rain fell. This procedure is reliable only over relatively smooth terrain having a substantial fraction of bare soil, such as exists in major agricultural regions during the dormant or early growing seasons. Soil moisture budgets were computed at selected sites to show how the observed emissivity responded to changes in the moisture content of the upper soil zone

Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction

This publication was made possible by NIH Grant P20 RR-17708-05 from the National Center for Research Resources of the National Institutes of Health. K.M.M. was a recipient of a National Institutes of Health Predoctoral Training Grant Fellowship (GM08545).PvdA catalyzes the hydroxylation of the sidechain primary amine of ornithine in the initial step of the biosynthesis of the Pseudomonas aeruginosa siderophore pyoverdin. The reaction requires FAD, NADPH, and O2. PvdA uses the same co-substrates as several flavin-dependent hydroxylases that differ one from another in the kinetic mechanisms of their oxidative and reductive half-reactions. Therefore, the mechanism of PvdA was determined by absorption stopped-flow experiments. By contrast to some flavin-dependent hydroxylases (notably, p-hydroxybenzoate hydroxylase), binding of the hydroxylation target is not required to trigger reduction of the flavin by NADPH: the reductive half-reaction is equally facile in the presence and absence of ornithine. Reaction of O2 with FADH2 in the oxidative half-reaction is accelerated by ornithine 80-fold, providing a mechanism by which PvdA can ensure coupling of NADPH and ornithine oxidation. In the presence of ornithine, the expected C(4a)-hydroperoxyflavin intermediate with 390-nm absorption accumulates and decays to the C(4a)-hydroxyflavin in a kinetically competent fashion. The slower oxidative half-reaction that occurs in the absence of ornithine involves accumulation of an oxygenated flavin species and two subsequent states that are tentatively assigned as C(4a)-peroxy- and -hydroperoxyflavin intermediates and the oxidized flavin. The enzyme generates stoichiometric hydrogen peroxide in lieu of hydroxyornithine. The data suggest that PvdA employs a kinetic mechanism that is a hybrid of those previously documented for other flavin-dependent hydroxylases

Provenance and depositional variability of the Thin Mud Facies in the lower Ganges-Brahmaputra delta,West Bengal Sundarbans, India

The Sundarbans is one of the largest coastal wetland sites in the world and covers an area of approximately one million hectares of the western delta of the Ganges and Brahmaputra (G-B) rivers (located across Bangladesh and India). Since the late Holocene, the western delta has not been directly fluvially sourced, due to the Ganges shift to the east (present-day Bangladesh). The depositional facies (Thin Mud Facies) of the late-Holocene abandoned western region (The Sundarbans) is derived from dominant estuary-tidal dynamics, however the provenance of the associated TMF sedimentation in this far western zone (Indian Sundarbans per se) is as yet equivocal. In this study, sediment cores from the Indian Sundarbans (Saptamukhi-Thakuran estuary) were closely examined for grain-size distributions (GSDs), mineralogy through X-ray diffraction (XRD), and geochemistry with X-ray fluorescence (XRF). The TMF in the West Bengal Sundarbans has been determined to show intensively weathered, terrestrial sediment, derived principally from the Ganges Alluvial Plain (GAP). There is a predominance of quartz, mica and clay minerals, with quartz interpreted as a product of low-relief tropical weathering sourced via the G-B Rivers draining the Himalayas. Lithofacies interpreted through GSD analysis of the TMF is indicative of a muddy tidal flat environment with aggradation and a general fining-up trend between the adjacent estuaries. The sediment provenance indicates a continuing G-B sediment source, which moves westward along the Bay of Bengal, from the active delta front and is then reworked over the far-western abandoned delta by tidal–estuarine forcing

Crystallographic Evidence of Drastic Conformational Changes in the Active Site of a Flavin-Dependent

The soil actinomycete Kutzneria sp. 744 produces a class of highly decorated hexadepsipeptides, which represent a new chemical scaffold that has both antimicrobial and antifungal properties. These natural products, known as kutznerides, are created via nonribosomal peptide synthesis using various derivatized amino acids. The piperazic acid moiety contained in the kutzneride scaffold, which is vital for its antibiotic activity, has been shown to derive from the hydroxylated product of l-ornithine, l-N5-hydroxyornithine. The production of this hydroxylated species is catalyzed by the action of an FAD- and NAD(P)H-dependent N-hydroxylase known as KtzI. We have been able to structurally characterize KtzI in several states along its catalytic trajectory, and by pairing these snapshots with the biochemical and structural data already available for this enzyme class, we propose a structurally based reaction mechanism that includes novel conformational changes of both the protein backbone and the flavin cofactor. Further, we were able to recapitulate these conformational changes in the protein crystal, displaying their chemical competence. Our series of structures, with corroborating biochemical and spectroscopic data collected by us and others, affords mechanistic insight into this relatively new class of flavin-dependent hydroxylases and adds another layer to the complexity of flavoenzymes.National Center for Research Resources (U.S.) (P41RR012408)National Institute of General Medical Sciences (U.S.) (P41GM103473