scholarly journals An abiotic source of Archean hydrogen peroxide and oxygen that pre-dates oxygenic photosynthesis

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Hongping He ◽  
Xiao Wu ◽  
Haiyang Xian ◽  
Jianxi Zhu ◽  
Yiping Yang ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Electron Donor ◽  
Redox State ◽  
Oxygenic Photosynthesis ◽  
Subsequent Generation

AbstractThe evolution of oxygenic photosynthesis is a pivotal event in Earth’s history because the O2 released fundamentally changed the planet’s redox state and facilitated the emergence of multicellular life. An intriguing hypothesis proposes that hydrogen peroxide (H2O2) once acted as the electron donor prior to the evolution of oxygenic photosynthesis, but its abundance during the Archean would have been limited. Here, we report a previously unrecognized abiotic pathway for Archean H2O2 production that involves the abrasion of quartz surfaces and the subsequent generation of surface-bound radicals that can efficiently oxidize H2O to H2O2 and O2. We propose that in turbulent subaqueous environments, such as rivers, estuaries and deltas, this process could have provided a sufficient H2O2 source that led to the generation of biogenic O2, creating an evolutionary impetus for the origin of oxygenic photosynthesis.

scholarly journals Novel homogeneous photocatalyst for oxygen to hydrogen peroxide reduction in aqueous media

2019 ◽  
Vol 18 (8) ◽  
pp. 1982-1989
Author(s):  
Daniil A. Lukyanov ◽  
Liya D. Funt ◽  
Alexander S. Konev ◽  
Alexey V. Povolotskiy ◽  
Anatoliy A. Vereshchagin ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Electron Donor ◽  
Aqueous Media ◽  
Peroxide Reduction ◽  
Hydrogen Peroxide Reduction

Novel pyrrolo-isoquinoline dyad was shown to be a promising photocatalyst for O2 to H2O reduction using oxalate as a sacrificial electron donor.

scholarly journals Production of hydrogen peroxide in the atmosphere of a Snowball Earth and the origin of oxygenic photosynthesis

2006 ◽  
Vol 103 (50) ◽  
pp. 18896-18899 ◽  
Author(s):  
M.-C. Liang ◽  
H. Hartman ◽  
R. E. Kopp ◽  
J. L. Kirschvink ◽  
Y. L. Yung
Keyword(s):  
Hydrogen Peroxide ◽  
Snowball Earth ◽  
Oxygenic Photosynthesis ◽  
Production Of Hydrogen

The modulation of thiol redox state affects the production and metabolism of hydrogen peroxide by heart mitochondria

2005 ◽  
Vol 441 (2) ◽  
pp. 112-122 ◽  
Author(s):  
Maria Pia Rigobello ◽  
Alessandra Folda ◽  
Guido Scutari ◽  
Alberto Bindoli
Keyword(s):  
Hydrogen Peroxide ◽  
Redox State ◽  
Heart Mitochondria ◽  
Thiol Redox State ◽  
Thiol Redox

Structure of a New Tetranuclear Iron(III) Complex with an Oxo-Bridge; Factors to Govern Formation and Stability of Oxo-Bridged Iron(III) Species in the L-Subunit of Ferritin

2006 ◽  
Vol 61 (1-2) ◽  
pp. 149-154 ◽  
Author(s):  
Yuichi Sutoh ◽  
Yuko Okawamukai ◽  
Satoshi Nishino ◽  
Yuzo Nishida
Keyword(s):  
Hydrogen Peroxide ◽  
Oxygen Atom ◽  
Electron Donor ◽  
Carboxyl Groups ◽  
Cavity Surface ◽  
Reaction Products ◽  
Ferroxidase Activity ◽  
Oxo Bridge

Abstract We have investigated the reaction products of several iron(III) compounds with hydrogen peroxide, and have found that hydrogen peroxide promotes the formation of an oxo-bridged iron(III) species in the presence of methanol (electron donor), and carboxyl groups of the ligand systems play a role to give the tetranuclear iron(III) compound containing a bent Fe- O-Fe unit (O: oxo oxygen atom). Based on the present results and the facts that L-chains of human ferritins lack ferroxidase activity, but are richer in carboxyl groups (glutamates) exposed on the cavity surface, it seems reasonable to conclude that (i) the hydrogen peroxide released in the H-subunit may contribute to the formation of a diferric oxo-hydrate in the L-subunit, (ii) the formation of a bent oxo-bridged iron(III) species is essentially important in the L-subunit, and (iii) rich carboxyl groups in L-subunits contribute to facilitate iron nucleation and mineralization through the capture and activation of the peroxide ion, and formation of a stable bent oxo-bridged iron(III) species

Dynamic measurements of mitochondrial hydrogen peroxide concentration and glutathione redox state in rat pancreatic β-cells using ratiometric fluorescent proteins: confounding effects of pH with HyPer but not roGFP1

2012 ◽  
Vol 441 (3) ◽  
pp. 971-978 ◽  
Author(s):  
Leticia P. Roma ◽  
Jessica Duprez ◽  
Hilton K. Takahashi ◽  
Patrick Gilon ◽  
Andreas Wiederkehr ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Redox State ◽  
Fluorescent Dyes ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Ph Sensitivity ◽  
Fluorescence Ratio ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Glutathione Redox

Using the ROS (reactive oxygen species)-sensitive fluorescent dyes dichlorodihydrofluorescein and dihydroethidine, previous studies yielded opposite results about the glucose regulation of oxidative stress in insulin-secreting pancreatic β-cells. In the present paper, we used the ratiometric fluorescent proteins HyPer and roGFP1 (redox-sensitive green fluorescent protein 1) targeted to mitochondria [mt-HyPer (mitochondrial HyPer)/mt-roGFP1 (mitochondrial roGFP1)] to monitor glucose-induced changes in mitochondrial hydrogen peroxide concentration and glutathione redox state in adenovirus-infected rat islet cell clusters. Because of the reported pH sensitivity of HyPer, the results were compared with those obtained with the mitochondrial pH sensors mt-AlpHi and mt-SypHer. The fluorescence ratio of the mitochondrial probes slowly decreased (mt-HyPer) or increased (mt-roGFP1) in the presence of 10 mmol/l glucose. Besides its expected sensitivity to H2O2, mt-HyPer was also highly pH sensitive. In agreement, changes in mitochondrial metabolism similarly affected mt-HyPer, mt-AlpHi and mt-SypHer fluorescence signals. In contrast, the mt-roGFP1 fluorescence ratio was only slightly affected by pH and reversibly increased when glucose was lowered from 10 to 2 mmol/l. This increase was abrogated by the catalytic antioxidant Mn(III) tetrakis (4-benzoic acid) porphyrin but not by N-acetyl-L-cysteine. In conclusion, due to its pH sensitivity, mt-HyPer is not a reliable indicator of mitochondrial H2O2 in β-cells. In contrast, the mt-roGFP1 fluorescence ratio monitors changes in β-cell mitochondrial glutathione redox state with little interference from pH changes. Our results also show that glucose acutely decreases rather than increases mitochondrial thiol oxidation in rat β-cells.

scholarly journals Peroxide processing in photosynthesis: antioxidant coupling and redox signalling

2000 ◽  
Vol 355 (1402) ◽  
pp. 1465-1475 ◽  
Author(s):  
Graham Noctor ◽  
Sonja Veljovic-Jovanovic ◽  
Christine H. Foyer
Keyword(s):  
Gene Expression ◽  
Complex System ◽  
Hydrogen Peroxide ◽  
Antioxidant System ◽  
Redox State ◽  
Redox Homeostasis ◽  
High Capacity ◽  
Control Of Gene Expression ◽  
Redox Signalling ◽  
Production Of Hydrogen

Photosynthesis has a high capacity for production of hydrogen peroxide (H 2 O 2 ), but the intracellular levels of this relatively weak oxidant are controlled by the antioxidant system, comprising a network of enzymatic and non-enzymatic components that notably includes reactions linked to the intracellular ascorbate and glutathione pools. Mutants and transformed plants with specific decreases in key components offer the opportunity to dissect the complex system that maintains redox homeostasis. Since H 2 O 2 is a signal-transducing molecule relaying information on intracellular redox state, the pool size must be rigorously controlled within each compartment of the cell. This review focuses on compartment-specific differences in the stringency of redox coupling between ascorbate and glutathione, and the significance this may have for the flexibility of the control of gene expression that is linked to photosynthetic H 2 O 2 production.

Photocatalytic Production of Hydrogen Peroxide by Tris(2,2‘-bipyridine) Ruthenium(II) Using Humic Acids as Electron Donor

1998 ◽  
Vol 32 (24) ◽  
pp. 3948-3953 ◽  
Author(s):  
Masami Fukushima ◽  
Kenji Tatsumi ◽  
Shunitz Tanaka ◽  
Hiroshi Nakamura
Keyword(s):  
Hydrogen Peroxide ◽  
Humic Acids ◽  
Electron Donor ◽  
Production Of Hydrogen
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