| List of contributing authors |
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XI | |
| Preface |
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XIII | |
| 1 Cyanobacterial design cell for the production of hydrogen from water |
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1 | (18) |
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1.1 Introduction: Why hydrogen producing cells? |
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1 | (2) |
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1.2 Antenna size reduction |
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3 | (2) |
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1.3 Partial uncoupling of ATP synthesis |
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5 | (2) |
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1.4 Re-directing electron flow at PS1-acceptor side |
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7 | (2) |
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1.5 Hydrogenase design strategies |
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9 | (2) |
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1.6 Photobioreactor design and continuous cultivation for optimization of design cell performance |
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11 | (3) |
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1.7 Outlook and biotechnological potential |
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14 | (5) |
| 2 Analysis and assessment of current photobioreactor systems for photobiological hydrogen production |
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19 | (22) |
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19 | (1) |
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2.2 Methodological approach |
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20 | (3) |
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23 | (1) |
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2.4 Sunlight-dependent hydrogen production rates |
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24 | (5) |
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29 | (8) |
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2.5.1 Life cycle inventory analysis |
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30 | (1) |
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2.5.2 Life cycle impact analysis |
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31 | (5) |
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36 | (1) |
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37 | (4) |
| 3 Catalytic properties and maturation of [ FeFe]-hydrogenases |
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41 | (20) |
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41 | (1) |
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3.2 The three major structure types of [ FeFe]-hydrogenases |
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41 | (1) |
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3.3 The H-cluster, the catalytic center of [ FeFe]-hydrogenases |
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42 | (1) |
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3.4 The catalytic cycle, a working hypothesis |
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43 | (2) |
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3.5 The interplay between H-cluster and protein environment |
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45 | (3) |
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3.6 Oxygen induced H-cluster degradation |
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48 | (2) |
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3.7 The native H-cluster maturation system |
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50 | (3) |
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3.8 Spontaneous in vitro maturation of the H-cluster |
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53 | (8) |
| 4 Oxygen-tolerant hydrogenases and their biotechnological potential |
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61 | (36) |
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61 | (2) |
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4.2 O2-tolerant membrane-bound hydrogenases |
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63 | (4) |
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4.2.1 Physiological function of O2-tolerant MBHs |
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63 | (1) |
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4.2.2 Structure and cofactor composition of O2-tolerant MBHs |
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64 | (2) |
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4.2.3 Mechanism of O2 tolerance in certain MBHs |
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66 | (1) |
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4.2.4 Proton reduction capacity of O2-tolerant MBHs |
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67 | (1) |
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4.3 O2-tolerant, NAD+-reducing hydrogenases |
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67 | (6) |
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4.3.1 Physiological function of NAD+-reducing hydrogenases |
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67 | (2) |
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4.3.2 Structure and reactivity of cofactors in NAD+-reducing hydrogenase |
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69 | (1) |
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4.3.3 Mechanism of O2 tolerance in NAD+-reducing hydrogenase |
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70 | (2) |
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4.3.4 Proton reduction capacity of NAD+-reducing hydrogenases |
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72 | (1) |
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4.4 O2-insensitive regulatory hydrogenases |
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73 | (8) |
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4.4.1 Genetic organization of hydrogenase genes and hydrogenase biosynthesis |
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73 | (3) |
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4.4.2 Role of the regulatory hydrogenase in H2-responsive signaling |
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76 | (2) |
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4.4.3 Unique features of regulatory hydrogenases |
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78 | (1) |
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4.4.4 The O2-insensitive regulatory hydrogenase as a major player in the O2-sensitive H2 signaling pathway |
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79 | (2) |
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4.5 O2-insensitive actinobacterial hydrogenases |
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81 | (5) |
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4.5.1 Physiological function of AHs |
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81 | (3) |
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4.5.2 Genetic organization of the AH operons |
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84 | (1) |
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4.5.3 AH cofactor composition and mechanism of O2 insensitivity |
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84 | (2) |
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4.6 Biotechnological application of O2-tolerant hydrogenases |
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86 | (1) |
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86 | (2) |
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88 | (9) |
| 5 Metal centers in hydrogenase enzymes studied by X-ray spectroscopy |
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97 | (30) |
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97 | (5) |
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5.2 X-ray spectroscopy results on hydrogenase proteins |
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102 | (14) |
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102 | (2) |
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5.2.2 [ FeFe]-hydrogenases |
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104 | (3) |
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5.2.3 [ NiFe]-hydrogenases |
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107 | (9) |
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5.2.4 [ NiFeSe]-hydrogenase |
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116 | (1) |
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5.3 Key questions in H2 chemistry and advanced X-ray techniques |
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116 | (11) |
| 6 Structure and function of [ Fe]-hydrogenase and biosynthesis of the FeGP cofactor |
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127 | (18) |
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127 | (1) |
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6.2 Physiological function |
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128 | (2) |
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6.2.1 Hydrogenases in methanogenesis |
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128 | (1) |
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129 | (1) |
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6.3 Structure of [ Fe]-hydrogenase |
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130 | (3) |
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130 | (2) |
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6.3.2 Structure of the FeGP cofactor |
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132 | (1) |
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133 | (4) |
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6.4.1 Reactions catalyzed |
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133 | (1) |
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134 | (1) |
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6.4.3 Catalytic mechanism |
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135 | (2) |
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6.5 Biosynthesis of the FeGP cofactor |
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137 | (4) |
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6.5.1 Stable-isotope labeling |
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137 | (2) |
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6.5.2 Hcg proteins involved in FeGP cofactor biosynthesis |
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139 | (2) |
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6.6 Potential application of [ Fe]-hydrogenase and the FeGP cofactor |
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141 | (4) |
| 7 Hydrogenase evolution and function in eukaryotic algae |
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145 | (28) |
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145 | (2) |
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7.2 Hydrogen production in green algae |
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147 | (3) |
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7.3 Hydrogen utilization pathways in green algae |
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150 | (1) |
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7.4 Hydrogenase activity, anaerobic metabolism and evolution |
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151 | (1) |
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7.5 Core anaerobic metabolisms in eukaryotes |
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152 | (1) |
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7.6 Fermentative H2 production in algae |
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153 | (1) |
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7.7 Disruption of fermentative enzymes in Chlamydomonas reinhardtii |
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153 | (3) |
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156 | (1) |
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7.9 [ FeFe]-hydrogenase assembly |
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157 | (2) |
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7.10 Algal hydrogenase diversity |
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159 | (4) |
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7.11 Hydrogenases in saltwater organisms |
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163 | (2) |
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165 | (8) |
| 8 Engineering of cyanobacteria for increased hydrogen production |
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173 | (16) |
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8.1 Native cyanobacteria, hydrogen production and hydrogen uptake |
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173 | (2) |
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8.2 Genetic engineering, synthetic biology |
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175 | (1) |
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8.3 Genetic engineering of cyanobacteria for enhanced hydrogen production |
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176 | (7) |
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8.3.1 Engineering of nitrogenases and hydrogenases for enhanced hydrogen production |
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177 | (5) |
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8.3.2 Genetic engineering of metabolic pathways for enhanced hydrogen production |
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182 | (1) |
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183 | (6) |
| 9 Semi-artificial photosynthetic Z-scheme for hydrogen production from water |
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189 | (22) |
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9.1 Nature-inspired approaches for hydrogen production |
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189 | (1) |
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9.2 Bio-photoelectrochemical half-cells based on photosynthetic proteins |
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190 | (7) |
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9.2.1 PS2-based photoanodes |
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191 | (2) |
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9.2.2 PS1-based photoelectrodes |
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193 | (4) |
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9.3 P51-catalyst nanoconstructs for hydrogen evolution |
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197 | (3) |
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198 | (1) |
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9.3.2 PS1-molecular wire-nanoparticle bioconjugates |
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198 | (1) |
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9.3.3 PS1-molecular wire-H2ase nanoconstructs |
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199 | (1) |
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9.3.4 PS1-H2ase hybrid complexes |
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200 | (1) |
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9.4 Electron transfer rates of PS1 in bio-photoelectrochemical devices and PS1-catalyst hybrids vs. natural photosynthesis |
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200 | (4) |
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9.5 Semi-artificial Z-scheme |
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204 | (2) |
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9.5.1 Realizing and exploiting a photosynthetic Z-scheme mimic for electrical energy production |
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204 | (1) |
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9.5.2 Improving the efficiency of a semi-artificial Z-scheme by adjusting the formal potential of the hydrogels |
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205 | (1) |
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9.6 Outlook P52-PS1-H2 catalyst |
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206 | (5) |
| 10 Photosynthesis and hydrogen metabolism revisited. On the potential of light-driven hydrogen production In vitro |
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211 | (28) |
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211 | (1) |
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10.2 Photosynthesis and redox balance |
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212 | (4) |
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10.2.1 Basic principles of photosynthetic electron transport |
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212 | (1) |
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10.2.2 Molecular structure of PSI and interaction with ferredoxin |
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213 | (3) |
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10.2.3 Light-driven hydrogen evolution |
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216 | (1) |
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10.3 Hydrogenases are the natural model of hydrogen catalysis |
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216 | (5) |
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10.3.1 The active site of [ NiFe]- and [ FeFe]-hydrogenases |
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217 | (1) |
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10.3.2 The structure of [ NiFe]- and [ FeFe]-hydrogenases |
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218 | (3) |
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10.4 Exploiting the modules of light-driven hydrogen production in vitro |
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221 | (8) |
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10.4.1 Nobel metal catalysis with PSI as photosensitizer |
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221 | (1) |
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10.4.2 Cluster-to-cluster electron wiring from PSI to hydrogenase |
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222 | (1) |
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10.4.3 Reconstitution of the PSI stromal ridge by a hydrogenase construct |
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223 | (6) |
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229 | (10) |
| 11 Re-routing redox chains for directed photocatalysis |
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239 | (26) |
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11.1 Making hydrogen with sunlight an alchemic approach |
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239 | (2) |
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11.2 Re-routing redox chains: Biological approaches |
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241 | (9) |
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11.2.1 Coating PSI with platinum |
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241 | (1) |
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11.2.2 Engineering PSI to interact with non-natural species |
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242 | (5) |
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247 | (3) |
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11.3 Re-routing redox chains: Synthetic approaches |
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250 | (6) |
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11.3.1 Artificial photosynthesis |
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251 | (3) |
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11.3.2 Hydrogenase active site mimics and alternative H2 production catalysts |
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254 | (1) |
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255 | (1) |
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11.4 Future directions and implications |
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256 | (9) |
| 12 Energy and entropy engineering on sunlight conversion to hydrogen using photosynthetic bacteria |
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265 | (12) |
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265 | (2) |
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12.1.1 Enthalpy to entropy |
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265 | (1) |
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12.1.2 The appropriate steps to the use of renewable energy |
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266 | (1) |
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12.2 Biological energy conversion methods as stabilizing elements of power grids |
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267 | (5) |
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12.2.1 Dark-fermentation in renewable energy systems |
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267 | (1) |
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12.2.2 Photo-fermentation in renewable energy systems |
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268 | (4) |
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272 | (5) |
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12.3.1 How to overcome the entropic difficulties of renewable energy sources by using biological functions |
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272 | (1) |
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12.3.2 Possible applications of biohydrogen in tropical regions |
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273 | (4) |
| Index |
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277 | |
Lisainfo e-raamatute kohta