Comparison of community structure of mangrove and riprap rock habitats along urban coastlines of south Florida

Globally, mangrove ecosystems have substantially declined, largely a result of human impacts. Mangroves provide a number of ecosystem services such as shoreline stabilization and nursery habitat for fish species. As declines continue, many of these ecosystem services are lost or altered. The need for shoreline stabilization has become increasingly apparent when chronic erosion wear away coastlines once mangroves are removed. Limestone boulders called riprap have been employed to offset continued erosion associated with mangrove clearing. In urban coastal areas adjacent to Biscayne Bay, Florida, as much as 80 percent of mangroves have been lost. More recently, riprap has been used in conjunction with mangroves to restore wetlands throughout the Bay. This riprap-mangrove habitat provides structure for marine organisms to colonize. However, fish assemblages and benthic composition could vary between this hybridized habitat and natural mangrove systems. Comparisons of fish and benthic community structure were made, to determine if abundance, species richness, and overall diversity differed between the two habitat types. Visual census and benthic quadrat surveys were conducted in vi mangrove and mangrove-riprap sites within two regions of Biscayne Bay. Total fish abundance was greater in mangroves, but the effect of habitat type on species richness varied between regions. The community structure of fishes and benthic composition differed significantly between mangroves and riprap habitats. Because species composition is so distinct, it is likely that the two communities do no function in the same manner. In areas with cleared shorelines, it may be important to consider the function of added anthropogenic structure for ecological communities.

Proton nuclear magnetic resonance investigation of the native and modified active site structure of heme proteins

Hemoproteins are a very important class of enzymes in nature sharing the essentially same prosthetic group, heme, and are good models for exploring the relationship between protein structure and function. Three important hemoproteins, chloroperoxidase (CPO), horseradish peroxidase (HRP), and cytochrome P450cam (P450cam), have been extensively studied as archetypes for the relationship between structure and function. In this study, a series of 1D and 2D NMR experiments were successfully conducted to contribute to the structural studies of these hemoproteins. ^ During the epoxidation of allylbenzene, CPO is converted to an inactive green species with the prosthetic heme modified by addition of the alkene plus an oxygen atom forming a five-membered chelate ring. Complete assignment of the NMR resonances of the modified porphyrin extracted and demetallated from green CPO unambiguously established the structure of this porphyrin as an NIII-alkylated product. A novel substrate binding motif of CPO was proposed from this concluded regiospecific N-alkylation structure. ^ Soybean peroxidase (SBP) is considered as a more stable, more abundant and less expensive substitute of HRP for industrial applications. A NMR study of SBP using 1D and 2D NOE methods successfully established the active site structure of SBP and consequently fills in the blank of the SBP NMR study. All of the hyperfine shifts of the SBP-CN- complex are unambiguously assigned together with most of the prosthetic heme and all proximal His170 resonances identified. The active site structure of SBP revealed by this NMR study is in complete agreement with the recombinant SBP crystal structure and is highly similar to that of the HRP with minor differences. ^ The NMR study of paramagnetic P450cam had been greatly restricted for a long time. A combination of 2D NMR methods was used in this study for P450cam-CN - complexes with and without camphor bound. The results lead to the first unequivocal assignments of all heme hyperfine-shifted signals, together with certain correlated diamagnetic resonances. The observed alternation of the assigned novel proximal cysteine β-CH2 resonances induced by camphor binding indicated a conformational change near the proximal side.^