Impact of temperature on the time required for the establishment of primordial biochemistry, and for the evolution of enzymes

被引:41
作者
Stockbridge, Randy B. [1 ]
Lewis, Charles A., Jr. [1 ]
Yuan, Yang [1 ]
Wolfenden, Richard [1 ]
机构
[1] Univ N Carolina, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA
基金
美国国家卫生研究院;
关键词
activation energy; thermophilic organisms; pyridoxal phosphate; phosphate ester hydrolysis; amino acid decarboxylation; CATALYTIC PROFICIENCIES; MANDELATE RACEMASE; BURDEN BORNE; HYDROLYSIS; KINETICS; WATER; CLEAVAGE; RATES; DECARBOXYLATION; PHOSPHODIESTER;
D O I
10.1073/pnas.1013647107
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
All reactions are accelerated by an increase in temperature, but the magnitude of that effect on very slow reactions does not seem to have been fully appreciated. The hydrolysis of polysaccharides, for example, is accelerated 190,000-fold when the temperature is raised from 25 to 100 degrees C, while the rate of hydrolysis of phosphate monoester dianions increases 10,300,000-fold. Moreover, the slowest reactions tend to be the most heat-sensitive. These tendencies collapse, by as many as five orders of magnitude, the time that would have been required for early chemical evolution in a warm environment. We propose, further, that if the catalytic effect of a "proto-enzyme"-like that of modern enzymes-were mainly enthalpic, then the resulting rate enhancement would have increased automatically as the environment became cooler. Several powerful nonenzymatic catalysts of very slow biological reactions, notably pyridoxal phosphate and the ceric ion, are shown to meet that criterion. Taken together, these findings greatly reduce the time that would have been required for early chemical evolution, countering the view that not enough time has passed for life to have evolved to its present level of complexity.
引用
收藏
页码:22102 / 22105
页数:4
相关论文
共 47 条
[1]   Microbial habitability of the Hadean Earth during the late heavy bombardment [J].
Abramov, Oleg ;
Mojzsis, Stephen J. .
NATURE, 2009, 459 (7245) :419-422
[2]   The kinetics of the spontaneous, proton- and AlIII-catalysed hydrolysis of 1,5-anhydrocellobiitol -: Models for cellulose depolymerization in paper aging and alkaline pulping, and a benchmark for cellulase efficiency [J].
Baty, JW ;
Sinnott, ML .
CANADIAN JOURNAL OF CHEMISTRY-REVUE CANADIENNE DE CHIMIE, 2005, 83 (09) :1516-1524
[3]   ENZYMATIC HYDRATION OF AN OLEFIN - THE BURDEN BORNE BY FUMARASE [J].
BEARNE, SL ;
WOLFENDEN, R .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (37) :9588-9589
[4]   Mandelate racemase in pieces: Effective concentrations of enzyme functional groups in the transition state [J].
Bearne, SL ;
Wolfenden, R .
BIOCHEMISTRY, 1997, 36 (07) :1646-1656
[5]   EXPRESSION PURIFICATION AND CHARACTERIZATION OF RECOMBINANT HUMAN N-ACETYLGALACTOSAMINE-6-SULFATASE [J].
BIELICKI, J ;
FULLER, M ;
GUO, XH ;
MORRIS, GP ;
HOPWOOD, JJ ;
ANSON, DS .
BIOCHEMICAL JOURNAL, 1995, 311 :333-339
[6]   Remarkably rapid cleavage of a model phosphodiester by complexed ceric ions in aqueous micellar solutions [J].
Bracken, K ;
Moss, RA ;
Ragunathan, KG .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (39) :9323-9324
[7]   TEMPERATURE DEPENDENCE OF STEADY STATE KINETICPARAMETERS OF FUMARASE REACTION [J].
BRANT, DA ;
BARNETT, LB ;
ALBERTY, RA .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1963, 85 (15) :2204-&
[8]   IMIDAZOLE CATALYSIS .1. THE CATALYSIS OF THE HYDROLYSIS OF PHENYL ACETATES BY IMIDAZOLE [J].
BRUICE, TC ;
SCHMIR, GL .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1957, 79 (07) :1663-1667
[9]   FACILE INTRAMOLECULAR HYDROLYSIS OF DIPEPTIDES AND GLYCINAMIDE [J].
BUCKINGHAM, DA ;
KEENE, FR ;
SARGESON, AM .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1974, 96 (15) :4981-4983
[10]   The burden borne by urease [J].
Callahan, BP ;
Yuan, Y ;
Wolfenden, R .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (31) :10828-10829