production from CO by an anerobic bacterial consortium [125]. Compared with
chemical nanoparticles, the biogenic ones are environmentally friendly and more
economical [132–134]. The presence of the biogenic nanoparticles increased the
CO solubility by more of 56% [125]. The CO solubility enhancement was attributed
to the sorption–desorption of CO gas bubbles on the surface of the nanoparticles
due to the presence of hydrophobic groups. The addition of biogenic iron
nanoparticles to the bioprocess allowed the maximum H 2 production of 30 mmol/L
[125].
The studies reported here reveal that hydrogen production through dark fermentation offers the best prospects for the development of a biohydrogen production process with high environmental benefits, contributing to clean energy
generation and waste utilization.
References
1. Navarro RM, Peña MA, Fierro JLG (2007) Hydrogen production reactions from carbon
feedstocks: fossil fuels and biomass. Chem Rev 107:4304–4330
2. De Lacey AL, Fernandez VM, Rousset M, Cammack R (2007) Activation and inactivation
of hydrogenase function and the catalytic cycle: spectroelectrochemical studies. Chem Rev
107:4304–4330
3. Fontecilla-Camps JC, Volbeda A, Cavazza C, Nicolet Y (2007) Structure/function
relationships of [NiFe]- and [FeFe]-hydrogenases. Chem Rev 107:4273–4303
4. Murphy BJ, Sargent F, Armstrong FA (2014) Transforming an oxygen-tolerant NiFe uptake
hydrogenase into a proficient, reversible hydrogen producer. Energy Environ Sci 7:1426–
1433
5. Hexter SV, Grey F, Happe T, Climent V, Armstrong FA (2012) Electrocatalytic mechanism
of reversible hydrogen cycling by enzymes and distinctions between the major classes of
hydrogenases. Proc Natl Acad Sci USA 109:18232–18233
6. Fourmond V, Baffert C, Sybirna K, Dementin S, Abou-Hamdan A, Meynial-Salles I,
Soucaille P, Bottin H, Leger C (2013) The mechanism of inhibition by H 2 of H 2 -evolution
by hydrogenases. Chem Commun 49:6840–6842
7. Kubas A, De Sancho D, Best RB, Blumberger J (2014) Aerobic damage to
FeFe-hydrogenases: activation barriers for the chemical attachment of O 2 . Angew Chem
Int Ed 53:4081–4084
8. Lu Y, Koo J (2019) O 2 sensitivity and H 2 production activity of hydrogenases—a review.
Biotechnol Bioeng 116:3124–3135
9. Roseboom W, DeLacey AL, Fernandez VM, Hatchikian EC, Albracht SPJ (2006) The active
site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light
sensitivity and CO-ligand exchange as observed by infrared spectroscopy. J Biol Inorg
Chem 11:102–118
10. Zorin NA, Gogotov IN, Kondratieva EN (1979) Hydrogen production by hydrogenase of
Alcaligenes eutrophus z-1 in the presence of oxygen. FEMS Microbiol Lett 5:301–304
11. Horch M, Lauterbach L, Mroginski MA, Hildebrandt P, Lenz O, Zebger I (2015) Reversible
active site sulfoxygenation can explain the oxygen tolerance of a NAD
+ -reducing [NiFe]
hydrogenase and its unusual infrared spectroscopic properties. J Am Chem Soc 137:2555–
2564
12. Inoue T, Kumar SN, Kamachi T, Okura I (1999) Hydrogen evolution from glucose with the
combination of glucose dehydrogenase and hydrogenase from A-eutrophus H16. Chem Lett
147–148
266
M. Martins et al.
chemical nanoparticles, the biogenic ones are environmentally friendly and more
economical [132–134]. The presence of the biogenic nanoparticles increased the
CO solubility by more of 56% [125]. The CO solubility enhancement was attributed
to the sorption–desorption of CO gas bubbles on the surface of the nanoparticles
due to the presence of hydrophobic groups. The addition of biogenic iron
nanoparticles to the bioprocess allowed the maximum H 2 production of 30 mmol/L
[125].
The studies reported here reveal that hydrogen production through dark fermentation offers the best prospects for the development of a biohydrogen production process with high environmental benefits, contributing to clean energy
generation and waste utilization.
References
1. Navarro RM, Peña MA, Fierro JLG (2007) Hydrogen production reactions from carbon
feedstocks: fossil fuels and biomass. Chem Rev 107:4304–4330
2. De Lacey AL, Fernandez VM, Rousset M, Cammack R (2007) Activation and inactivation
of hydrogenase function and the catalytic cycle: spectroelectrochemical studies. Chem Rev
107:4304–4330
3. Fontecilla-Camps JC, Volbeda A, Cavazza C, Nicolet Y (2007) Structure/function
relationships of [NiFe]- and [FeFe]-hydrogenases. Chem Rev 107:4273–4303
4. Murphy BJ, Sargent F, Armstrong FA (2014) Transforming an oxygen-tolerant NiFe uptake
hydrogenase into a proficient, reversible hydrogen producer. Energy Environ Sci 7:1426–
1433
5. Hexter SV, Grey F, Happe T, Climent V, Armstrong FA (2012) Electrocatalytic mechanism
of reversible hydrogen cycling by enzymes and distinctions between the major classes of
hydrogenases. Proc Natl Acad Sci USA 109:18232–18233
6. Fourmond V, Baffert C, Sybirna K, Dementin S, Abou-Hamdan A, Meynial-Salles I,
Soucaille P, Bottin H, Leger C (2013) The mechanism of inhibition by H 2 of H 2 -evolution
by hydrogenases. Chem Commun 49:6840–6842
7. Kubas A, De Sancho D, Best RB, Blumberger J (2014) Aerobic damage to
FeFe-hydrogenases: activation barriers for the chemical attachment of O 2 . Angew Chem
Int Ed 53:4081–4084
8. Lu Y, Koo J (2019) O 2 sensitivity and H 2 production activity of hydrogenases—a review.
Biotechnol Bioeng 116:3124–3135
9. Roseboom W, DeLacey AL, Fernandez VM, Hatchikian EC, Albracht SPJ (2006) The active
site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light
sensitivity and CO-ligand exchange as observed by infrared spectroscopy. J Biol Inorg
Chem 11:102–118
10. Zorin NA, Gogotov IN, Kondratieva EN (1979) Hydrogen production by hydrogenase of
Alcaligenes eutrophus z-1 in the presence of oxygen. FEMS Microbiol Lett 5:301–304
11. Horch M, Lauterbach L, Mroginski MA, Hildebrandt P, Lenz O, Zebger I (2015) Reversible
active site sulfoxygenation can explain the oxygen tolerance of a NAD
+ -reducing [NiFe]
hydrogenase and its unusual infrared spectroscopic properties. J Am Chem Soc 137:2555–
2564
12. Inoue T, Kumar SN, Kamachi T, Okura I (1999) Hydrogen evolution from glucose with the
combination of glucose dehydrogenase and hydrogenase from A-eutrophus H16. Chem Lett
147–148
266
M. Martins et al.