CALCULATION OF THERMODYNAMIC PROPERTIES OF PROTEIN IN ESCHERICHIA-COLI-K-12 GROWN ON SUCCINIC ACID, ENERGY CHANGES ACCOMPANYING PROTEIN ANABOLISM, AND ENERGETIC ROLE OF ATP IN PROTEIN-SYNTHESIS

被引:10
作者
BATTLEY, EH
机构
[1] Department of Ecology and Evolution, State University of New York at Stony Brook, Stony Brook, New York
关键词
FREE ENERGY OF PROTEIN FORMATION; ENTHALPY OF PROTEIN FORMATION; ENTROPY OF PROTEIN FORMATION; ENERGIES OF PROTEIN ANABOLISM; ATP ENERGY CONSERVATION IN PROTEIN;
D O I
10.1002/bit.260400212
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Using an average of the results from three methods of calculation, estimations are made of the thermodynamic properties of a unit carbon formula weight (UCFW) of Escherichia coli K-12 protein. These resulted in values for DELTA-G(f) of -38.09 kJ (-9.10 kcal)/UCFW, for DELTA-H(f) of -68.18 kJ (-16.29 kcal)/UCFW, and for DELTA-S(f) of -94.2 J (-22.5 cal)/UCFW deg. The absolute entropy of one UCFW of E. coli K-12 protein is calculated to be 73.8 J/UCFW deg. Using these values, the corresponding changes in thermodynamic properties accompanying the anabolism of protein by this microorganism to form one UCFW of protein are calculated to be 1.97 kJ (047 kcal)/UCFW for DELTA-G, 0.75 kJ (0.18 kcal)/UCFW for DELTA-H, and -4.09 J (-0.98 cal)/UCFW deg for DELTA-S. All these values are sufficiently close to zero that they may be considered to be so. The question is raised as to the quantity of ATP energy conserved within the substance of the protein as it is synthesized from succinic acid. It is calculated that only 3.8% of the total free energy available from ATP that is required during protein anabolism can have been conserved within the substance of the protein, there being a net conversion of the remainder into heat and entropy.
引用
收藏
页码:280 / 288
页数:9
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