Apr 14, 2014

Average oxidation state of carbon in proteins

BioRxiv : the Preprint Server for Biology
Jeffrey M Dick

Abstract

The degree of oxidation of carbon atoms in organic molecules depends on the covalent structure. In proteins, the average oxidation state of carbon ( Z C) can be calculated as an elemental ratio from the chemical formula. To investigate oxidation-reduction (redox) patterns, groups of proteins from different subcellular locations and phylogenetic divisions were selected for comparison. Extracellular proteins of yeast have a relatively high oxidation state of carbon, corresponding with oxidizing conditions outside of the cell. However, an inverse relationship between Z C and redox potential occurs between the endoplasmic reticulum and cytoplasm; this trend is interpreted as resulting from overall coupling of protein turnover to the formation of a lower glutathione redox potential in the cytoplasm. In Rubisco homologues, lower Z C tends to occur in organisms with higher optimal growth temperature, and there are broad changes in Z C in whole-genome protein compositions in microbes from different environments. Energetic costs calculated from thermodynamic models suggest that thermophilic organisms exhibit molecular adaptation to not only high temperature but also the reducing nature of many hydrothermal fluids. A view of protein meta...Continue Reading

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Mentioned in this Paper

Covalent Interaction
Patterns
Genome
Extracellular
Environment
Protein Metabolism Process
Yeasts
Protein Degradation, Metabolic
Glutathione Measurement
Carbon

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