A new metric for sunlight exposure in rivers, lakes, and oceans

Abstract Vertical motion is an important driver of sunlight exposure in aquatic environments, shaping the growth and fate of materials and organisms. We derive a simple model accounting for turbulent depth fluctuations of particles to predict the depth that contributes the most sunlight exposure (effective depth) as well as the single depth that, if measured at one place over time, produces the same total sunlight exposure as a moving particle (functional depth). Field measurements of light and depth in rivers using neutrally buoyant drifters and buoys validate our model. Effective depth varied from 0.1 to 1.5 m below the water surface and was ~ 30% of the overall water depth on average. Functional depth varied from 0.67 to 2.3 m and was ~ 50% of the overall water depth on average. Functional and effective depth are physically based concepts incorporating turbulent motion, spatial variability, and water clarity offering new approaches to characterize light exposure in aquatic environments

On the structure of the nickel/iron/sulfur center of the carbon monoxide dehydrogenase from Rhodospirillum rubrum: An x-ray absorption spectroscopy study

The nickel/iron/sulfur center of the carbon monoxide dehydrogenase (carbon monoxide: (acceptor)oxidoreductase; EC 1.2.99.2) enzyme from Rhodospirillum rubrum (Rr-CODH) was studied by x-ray absorption spectroscopy at the Ni K edge. Extended x-ray absorption fine structure data show that the first Ni coordination shell consists of 2 S atoms at 2.23 Å and 2-3 N/O atoms at 1.87 Å. The edge structure indicates a distorted tetrahedral or five-coordinate Ni environment in both oxidized and reduced Rr-CODH. By comparing second-shell extended x-ray absorption fine structure data of Rr-CODH to that of (Et4N)3[NiFe3S4(SEt)4], a cubane-type cluster, it was clearly established that Ni in the Rr-CODH center is not involved in the core of a NiFe3S4 cubane cluster. One model consistent with the results is a mononuclear Ni2+ site, bridged by S-Cys or sulfide to one or both of the Fe4S4 clusters of the enzyme, with the remaining coordination sites occupied by additional S-Cys or N/O-liganding amino acid residues

Temperature Dependence of Water Interactions with the Amide Carbonyls of α-Helices

[Image: see text] Hydration is a key determinant of the folding, dynamics, and function of proteins. In this study, temperature-dependent Fourier transform infrared (FTIR) spectroscopy combined with singular value decomposition (SVD) and global fitting were used to investigate both the interaction of water with α-helical proteins and the cooperative thermal unfolding of these proteins. This methodology has been applied to an isolated α-helix (Fs peptide) and to globular α-helical proteins including the helical subdomain and full-length villin headpiece (HP36 and HP67). The results suggest a unique IR signature for the interaction of water with the helical amide carbonyl groups of the peptide backbone. The IR spectra indicate a weakening of the net hydrogen bond strength of water to the backbone carbonyls with increasing temperature. This weakening of the backbone solvation occurs as a discrete transition near the maximum of the temperature-dependent hydrophobic effect, not a continuous change with increasing temperature. Possible molecular origins of this effect are discussed with respect to previous molecular dynamics simulations of the temperature-dependent solvation of the helix backbone