Large impacts, past and future, of ozone-depleting substances on Brewer-Dobson circulation trends: A multi-model assessment.

Substantial increases in the atmospheric concentration of well-mixed greenhouse gases (notably CO2), such as those projected to occur by the end of the 21st century under large radiative forcing scenarios, have long been known to cause an acceleration of the Brewer-Dobson circulation (BDC) in climate models. More recently, however, several single-model studies have proposed that ozone-depleting substances might also be important drivers of BDC trends. As these studies were conducted with different forcings over different periods, it is difficult to combine them to obtain a robust quantitative picture of the relative importance of ozone-depleting substances as drivers of BDC trends. To this end we here analyze - over identical past and future periods - the output from 20 similarly-forced models, gathered from two recent chemistry-climate modeling intercomparison projects. Our multi-model analysis reveals that ozone-depleting substances are responsible for more than half of the modeled BDC trends in the two decades 1980-2000. We also find that, as a consequence of the Montreal Protocol, decreasing concentrations of ozone-depleting substances in coming decades will strongly decelerate the BDC until the year 2080, reducing the age-of-air trends by more than half, and will thus substantially mitigate the impact of increasing CO2. As ozone-depleting substances impact BDC trends, primarily, via the depletion/recovery of stratospheric ozone over the South Pole, they impart seasonal and hemispheric asymmetries to the trends which may offer opportunities for detection in coming decades.

Ozone-climate interactions and effects on solar ultraviolet radiation.

This report assesses the effects of stratospheric ozone depletion and anticipated ozone recovery on the intensity of ultraviolet (UV) radiation at the Earth's surface. Interactions between changes in ozone and changes in climate, as well as their effects on UV radiation, are also considered. These evaluations focus mainly on new knowledge gained from research conducted during the last four years. Furthermore, drivers of changes in UV radiation other than ozone are discussed and their relative importance is assessed. The most important of these factors, namely clouds, aerosols and surface reflectivity, are related to changes in climate, and some of their effects on short- and long-term variations of UV radiation have already been identified from measurements. Finally, projected future developments in stratospheric ozone, climate, and other factors affecting UV radiation have been used to estimate changes in solar UV radiation from the present to the end of the 21st century. New instruments and methods have been assessed with respect to their ability to provide useful and accurate information for monitoring solar UV radiation at the Earth's surface and for determining relevant exposures of humans. Evidence since the last assessment reconfirms that systematic and accurate long-term measurements of UV radiation and stratospheric ozone are essential for assessing the effectiveness of the Montreal Protocol and its Amendments and adjustments. Finally, we have assessed aspects of UV radiation related to biological effects and human health, as well as implications for UV radiation from possible solar radiation management (geoengineering) methods to mitigate climate change.

Small interannual variability of global atmospheric hydroxyl.

The oxidizing capacity of the global atmosphere is largely determined by hydroxyl (OH) radicals and is diagnosed by analyzing methyl chloroform (CH(3)CCl(3)) measurements. Previously, large year-to-year changes in global mean OH concentrations have been inferred from such measurements, suggesting that the atmospheric oxidizing capacity is sensitive to perturbations by widespread air pollution and natural influences. We show how the interannual variability in OH has been more precisely estimated from CH(3)CCl(3) measurements since 1998, when atmospheric gradients of CH(3)CCl(3) had diminished as a result of the Montreal Protocol. We infer a small interannual OH variability as a result, indicating that global OH is generally well buffered against perturbations. This small variability is consistent with measurements of methane and other trace gases oxidized primarily by OH, as well as global photochemical model calculations.

Coupling mechanism of the oxaloacetate decarboxylase Na(+) pump.

The oxaloacetate decarboxylase Na(+) pump consists of subunits alpha, beta and gamma, and contains biotin as the prosthetic group. The peripheral alpha subunit catalyzes the carboxyltransfer from oxaloacetate to the prosthetic biotin group to yield the carboxybiotin enzyme. Subsequently, this is decarboxylated in a Na(+)-dependent reaction by the membrane-bound beta subunit. The decarboxylation is coupled to Na(+) translocation from the cytoplasm into the periplasm, and consumes a periplasmically derived proton. The gamma subunit contains a Zn(2+) metal ion which may be involved in the carboxyltransfer reaction. It is proposed to insert with its N-terminal alpha-helix into the membrane and to form a complex with the alpha subunit with its water-soluble C-terminal domain. The beta subunit consists of nine transmembrane alpha-helices, a segment (IIIa) which inserts from the periplasm into the membrane but does not penetrate it, and connecting hydrophilic loops. The most highly conserved regions of the molecule are segment IIIa and transmembrane helix VIII. Functionally important residues are D203 (segment IIIa), Y229 (helix IV) and N373, G377, S382 and R389 (helix VIII). The polar of these amino acids may constitute a network of ionizable groups which promotes the translocation of Na(+) and the oppositely oriented translocation of H(+) across the membrane. Evidence indicates that two Na(+) ions are bound simultaneously to subunit beta with D203 and S382 acting as binding sites. Sodium ion binding from the cytoplasm to both sites elicits decarboxylation of carboxybiotin possibly with the consumption of the proton extracted from S382 and delivered via Y229 to the carboxylated prosthetic group. A conformational change exposes the bound Na(+) ions toward the periplasm. With H(+) entering from the periplasm, the hydroxyl group of S382 is regenerated, and as a consequence, the Na(+) ions are released into this compartment. After switching back to the original conformation, Na(+) pumping continues.

Essential role of tyrosine 229 of the oxaloacetate decarboxylase beta-subunit in the energy coupling mechanism of the Na(+) pump.

The membrane-bound beta-subunit of oxaloacetate decarboxylase from Klebsiella pneumoniae catalyzes the decarboxylation of carboxybiotin, which is coupled to Na(+) translocation and consumes a periplasmically derived proton. Upon site-directed mutagenesis of 20 polar and/or conserved residues within putative membrane-integral regions, the specific oxaloacetate decarboxylase activities were reduced to various extents, but only the enzyme with a Y229F mutation was completely inactive. We propose that Y229 is part of the network by which the proton of S382 is delivered to carboxybiotin, where it is consumed upon catalyzing the immediate decarboxylation of this acid-labile compound. Unlike S382 or D203, Y229 appears to be not involved in Na(+) binding, because in the Y229F orY229A mutants, the beta-subunit was protected from tryptic digestion by 50 mM NaCl like in the wild-type enzyme. Oxaloacetate decarboxylase with a betaC291E mutation was unstable in the absence of Na(+) and dissociated into an alpha-gamma subcomplex and the beta-subunit. The enzyme could only be isolated in the presence of 0. 5 M NaCl. These results are consistent with the notion that the beta-subunit changes its conformation upon Na(+) binding.

A molecular coupling mechanism for the oxaloacetate decarboxylase Na+ pump as inferred from mutational analysis.

The oxaloacetate decarboxylase Na+ pump consists of subunits alpha, beta, and gamma, and contains biotin as the prosthetic group. Membrane-bound subunit beta catalyzes the decarboxylation of carboxybiotin coupled to Na+ translocation, and consumes a periplasmically derived proton. Site-directed mutagenesis of conserved amino acids of transmembrane helix VIII indicated that residues N373, G377, S382, and R389 are functionally important. The polar side groups of these amino acids may constitute together with D203 a network of ionizable groups which promotes the translocation of Na+ and the oppositely oriented H+ across the membrane. Evidence is presented that two Na+ ions are bound simultaneously to subunit beta during transport with D203 and S382 acting as binding sites. Sodium ion binding from the cytoplasm to both sites elicits decarboxylation of carboxybiotin, and a conformational switch exposes the bound Na+ ions toward the periplasm. After dissociation of Na+ and binding of H+, the cytoplasmically exposed conformation is regained.

Membrane topology of the beta-subunit of the oxaloacetate decarboxylase Na+ pump from Klebsiella pneumoniae.

The topology of the beta-subunit of the oxaloacetate Na+ pump (OadB) was probed with the alkaline phosphatase (PhoA) and beta-galactosidase (lacZ) fusion technique. Additional evidence for the topology was derived from amino acid alignments and comparative hydropathy profiles of OadB with related proteins. Consistent results were obtained for the three N-terminal and the six C-terminal membrane-spanning alpha-helices. However, the two additional helices that were predicted by hydropathy analyses between the N-terminal and C-terminal blocks did not conform with the fusion results. The analyses were therefore extended by probing the sideness of various engineered cysteine residues with the membrane-impermeant reagent 4-acetamido-4'-maleimidylstilbene-2, 2'-disulfonate. The results were in accord with those of the fusion analyses, suggesting that the protein folds within the membrane by a block of three N-terminal transmembrane segments and another one with six C-terminal transmembrane segments. The mainly hydrophobic connecting segment is predicted not to traverse the membrane fully, but to insert in an undefined manner from the periplasmic face. According to our model, the N-terminus is at the cytoplasmic face and the C-terminus is at the periplasmic face of the membrane.