calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring计算相对蛋白质作为温度的函数的化学稳定性和氧化还原化学温泉.pdfVIP

Calculation of the Relative Chemical Stabilities of Proteins as a Function of Temperature and Redox Chemistry in a Hot Spring 1 1,2 Jeffrey M. Dick *, Everett L. Shock 1 School of Earth and Space Exploration, Arizona State University, Tempe, Arizona, United States of America, 2 Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona, United States of America Abstract Uncovering the chemical and physical links between natural environments and microbial communities is becoming increasingly amenable owing to geochemical observations and metagenomic sequencing. At the hot spring known as Bison Pool in Yellowstone National Park, the cooling of the water in the outflow channel is associated with an increase in oxidation potential estimated from multiple field-based measurements. Representative groups of proteins whose sequences were derived from metagenomic data also exhibit an increase in average oxidation state of carbon in the protein molecules with distance from the hot-spring source. The energetic requirements of reactions to form selected proteins used in the model were computed using amino-acid group additivity for the standard molal thermodynamic properties of the proteins, and the relative chemical stabilities of the proteins were investigated by varying temperature, pH and oxidation state, expressed as activity of dissolved hydrogen. The relative stabilities of the proteins were found to track the locations of the sampling sites when the calculations included a function for hydrogen activity that increases with temperature and is higher, or more reducing, than values consistent with measurements of dissolved oxygen, sulfide and oxidation-reduction potential in the field. These findings imply that spatial pat