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Phosphorus chemistry : the role of phosphorus in prebiotic chemistry / Yufen Zhao [and 3 others].

Chemistry Library - Books QD181.P1 Z43 2019
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Format:
Book
Author/Creator:
Zhao, Yufen, 1948- author.
Language:
English
Subjects (All):
Phosphorus.
Phosphorus--Metabolism.
Physical Description:
xv, 166 pages : illustrations (some color) ; 25 cm
Place of Publication:
Berlin/Boston : De Gruyter : Xiamen University Press, [2019]
Contents:
1 The international background of the origin of life p. 1
1.1 Original source of phosphorus p. 1
1.1.1 Nuclear reactions p. 1
1.1.2 Phosphorus surrounds celestial interval and interstellar space p. 2
1.1.3 Phosphorus in meteorites p. 2
1.1.4 Phosphorus in comets p. 3
1.1.5 Alkyl phosphoric acid homologues p. 3
1.1.6 Phosphorus in the crust p. 3
1.1.7 Phosphorylation under prebiological conditions p. 4
1.2 Phosphorus and small biomolecules p. 5
1.2.1 Formation of amino acids with phosphorus p. 5
1.2.2 Formation of bases p. 5
1.2.3 Formation of nucleosides with phosphorus p. 6
1.2.4 Formation of nucleotides p. 7
1.3 Phosphorus and biomacromolecules p. 9
1.3.1 Formation of peptides with phosphorus p. 9
1.3.2 Nucleic acid pre-biosynthesis p. 10
1.4 Irreplaceability of phosphorus in life p. 14
1.5 Subject of the origin of life p. 14
2 Why nature chose α-ammo acids? p. 19
2.1 Amino acids and the origins of life p. 19
2.2 General structures of amino acids and the biological functions p. 20
2.3 Prebiotic formation of amino acids p. 21
2.4 Prebiotic formation of peptides p. 23
2.5 Phosphorus chemistry for prebiotic peptide formation p. 24
2.5.1 Reaction of amino acids with trimetaphosphate p. 25
2.5.2 Peptide formation of N-phosphoryl amino acids p. 28
2.5.3 Peptide formation mediated by organic phosphorus reagents p. 31
2.6 Phosphorus chemistry and the molecular evolution of high-energy P-N bond p. 33
3 N-Phosphoryl amino acids - models for P-N bonds in prebiotic chemical evolution p. 35
3.2 The P-N bond in modern biology p. 36
3.2.1 Phosphohistidsne p. 37
3.2.2 Phosphoarginine and phosphoryl-lysine p. 37
3.3 Potential prebiotic origins of N-α-phosphoryl amino acids p. 38
3.3.1 The phosphorus problem p. 38
3.3.2 Possible pathways for origin of N-phosphoryl amino acids p. 39
3.4 Reactivity of Nα-phosphoryl amino acids related to prebiotic chemistry p. 40
3.4.1 N-dialkyloxyphosphoryl amino acids p. 40
3.4.2 NMAPAAs p. 43
3.4.3 N-phosphono-amino acids p. 45
4 Nucleoside-proteln coevolutaon and the origin of genetic code p. 53
4.1 Major phase in the origin of life p. 53
4.2 Origin of genetic code p. 55
4.3 The evolution of genetic code p. 57
4.4 Phosphorus plays an important role in the origin of life p. 59
4.5 N-phosphoryl amino acids: model for the study of nucleotide-protein coevolution p. 61
4.6 The relationship of dipeptide yields with nucleoside in the phosphorus-assisted condensation of amino acids p. 62
5 The phosphoryl transfer reactions of pentacoordinated phosphoryl amino acids p. 67
5.1 The research progress of phosphoryl transfer reaction p. 67
5.2 Study on the transfer reaction of Intermolecular O,O-Phenylenephosphoryl group p. 69
5.2.1 Synthesis and analysis of Ser-His dipeptide p. 69
5.2.2 The investigation of the intermolecular transfer mechanism of O,O-phenylenephosphoryl group between amino acids p. 71
5.3 The transfer reaction of N-(O,O-diisopropyl) phosphoryl between different ammo acids p. 74
5.4 The studies on the phosphoryl transfer reaction between different types of amino acids p. 76
6 The research progress of chiral pentacoordinate spirophosphoranes with bis-α-amino acid bonds p. 81
6.1 The importance of pentacoordinate phosphorus compounds in biological processes p. 81
6.2 The synthesis method of chiral pentacoordinate spirophosphoranes p. 82
6.3 Spectroscopic characterization of bisamino acyl pentacoordinate spirophosphoranes p. 85
6.3.1 ⁴JH-C-N-P-H p. 85
6.3.2 ¹JP-X p. 88
6.3.3 X-ray p. 90
6.3.4 Solid-state CD spectra p. 93
7 A new theoretical model for the origin of amino acid homochirality p. 99
7.1 The origin of homochirality p. 99
7.2 Model for the origin of amino acid homochirality p. 100
7.3 Interaction of nucleosides and amino acids p. 101
7.4 Thermodynamic parameters of interaction between nucleosides and amino acids p. 104
8 N-Phosphoryl amino acids and the origin of cell membranes p. 109
8.1 The origin and evolution of cells p. 109
8.1.1 The formation of primitive cells - The beginning of the music of life p. 109
8.1.2 The formation of prokaryotic and eukaryotic cell p. 110
8.2 Membrane structures constructed by amphiphilic N-phospboryl amino acids p. 110
8.2.1 Synthesis of amphiphilic N-phosphoryl amino acids p. 112
8.2.2 Self-assembled monolayers of amphiphilic N-phosphoryl amino acids at water-air interface and their condensation reactions p. 112
8.2.2.1 Formation of monomolecular membranes from amphiphilic N-phosphoryl amino acids at the water-air interface p. 112
8.2.2.2 Condensation of amphiphilic N-phosphoryl amino acids at the water-air interface p. 114
8.2.3 Formation and reaction of bimolecular membranes-vesicles in water by amphiphilic N-phosphoryl amino acids p. 116
8.2.3.1 Formation and characterization of vesicles p. 116
8.2.3.2 Condensation in vesicle systems p. 118
8.3 Evolution of the protocell membrane p. 120
8.4 N-Phosphoryl amino acids and the origin of life p. 121
8.4.1 Synergistic effect of membrane, nucleic acid and protein p. 121
8.4.2 The coevolution theory of nucleic acid, protein and cell membrane p. 121
9 The potential evolution prototype of modern enzyme: Discovery of seryl-histidine dipeptide and its function p. 125
9.1 Mini-activating enzyme: Ser-His p. 125
9.2 The cleavage activities of Ser-His on DNA p. 126
9.2.1 Discovery of the hydrolysis activity of Ser-His on DHA p. 126
9.2.2 The cleavage mechanism of Ser-His on DNA and the pivotal role of functional groups in Ser-His p. 127
9.2.3 Molecular modeling for investigating DNA cleavage activity of Ser-His p. 129
9.3 The cleavage activities of Ser-His on proteins p. 130
9.3.1 The discovery of the cleavage activities of Ser-His on proteins p. 130
9.3.2 The effect of different buffers on the cleavage activities p. 131
9.3.3 The role of functional groups of Ser-His in the cleavage activities p. 131
9.3.4 The study of the interaction of Ser-His with the substrate proteins p. 132
9.3.5 The cleavage activities of Ser-His on carboxylic ester p. 134
9.3.6 The functional reversibility of Ser-His on the substrate p. 134
9.4 Ser-His: the evolution prototype of modern enzyme p. 135
10 The interaction between ATP and amino acids p. 141
10.1 The study of the origin and evolution of protein based on small molecule p. 141
10.1.1 ATP - a living fossil at the molecular level p. 141
10.1.2 ATP-bindingprotein -the oldest protein p. 142
10.2 The structure and the interaction with AAs of ATP p. 145
10.2.1 The structure of ATP p. 145
10.2.2 Study on the weak interaction between AA and ATP by MS p. 146
10.23 Study on the weak interaction between AA and ATP by fluorescence spectrometry p. 149
10.2.4 Study of the weak interaction between AA and ATP by NMR p. 150
10.2.5 Study of the weak interaction between AA and ATP by theoretical calculation p. 151
10.2.6 The interaction between AA and ATP p. 154
11 Marine and the origin of life p. 157
11.1 The Origin of Life p. 157
11.2 The origin of marine life p. 158
11.2.1 The theory of the origin of marine life p. 158
11.2.2 Simulation of chemical evolution of marine life p. 159
11.3 Phosphate oxygen isotope as a biomarker p. 160
11.3.1 The oxygen isotope fractionation between water and phosphate p. 161
11.3.1.1 Oxygen isotope fractionation between water and biotic apatite p. 161
11.3.1.2 Oxygen isotope fractionation between water and authigenic apatite p. 162
11.3.1.3 Oxygen isotope fractionation between water and dissolved phosphate p. 163
11.3.2 The application of oxygen isotope composition of phosphate p. 164
11.3.2.1 The primary value of the oxygen isotope composition of phosphate p. 164
11.3.2.2 The review of the phosphate oxygen isotope biomarker p. 164.
Notes:
Includes bibliographical references.
ISBN:
3110562375
9783110562378
OCLC:
1028883511

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