[FeFe]-Hydrogenases: maturation and reactivity of enzymatic systems and overview of biomimetic models

2021 ◽  
Author(s):  
Julian T. Kleinhaus ◽  
Florian Wittkamp ◽  
Shanika Yadav ◽  
Daniel Siegmund ◽  
Ulf-Peter Apfel
Keyword(s):  
Biomimetic Models ◽  
Enzymatic Systems

[FeFe]-hydrogenases recieved increasing interest in the last decades. This review summarises important findings regarding their enzymatic reactivity as well as inorganic models applied as electro- and photochemical catalysts.

scholarly journals Human Osteochondral Explants: Reliable Biomimetic Models to Investigate Disease Mechanisms and Develop Personalized Treatments for Osteoarthritis

2021 ◽  
Author(s):  
Evelyn Houtman ◽  
Marcella van Hoolwerff ◽  
Nico Lakenberg ◽  
Eka H. D. Suchiman ◽  
Enrike van der Linden-van der Zwaag ◽  
...  
Keyword(s):  
Biomimetic Models ◽  
Disease Mechanisms

Oxidative Activity of Aortic Tissue of Man, the Rabbit and the Dog, With Special Reference to Succinic Dehydrogenase and Cytochrome Oxidase

1958 ◽  
Vol 195 (2) ◽  
pp. 476-480 ◽  
Author(s):  
Nelicia Maier ◽  
Henry Haimovici
Keyword(s):  
Special Reference ◽  
Cytochrome Oxidase ◽  
Abdominal Aorta ◽  
Abdominal Segment ◽  
Species Difference ◽  
Succinic Dehydrogenase ◽  
Hepatic Tissue ◽  
Human Aorta ◽  
Aortic Tissue ◽  
Enzymatic Systems

Succinic dehydrogenase and cytochrome oxidase activities were determined in homogenates of three aortic segments (ascending and arch, descending thoracic, abdominal) and liver of man, the rabbit and the dog. Both enzymes exhibited the lowest activity in human aorta. Succinic dehydrogenase exhibited the highest activity in the thoracic aorta of the dog and intermediate activity in the latter's abdominal segment and the rabbit's aorta. Cytochrome oxidase, in contrast, exhibited the highest activity in the rabbit's aorta. A slight gradient of decreasing activity from thoracic to abdominal aorta was noted for cytochrome oxidase in both the rabbit and dog and for succinic dehydrogenase in the rabbit, whereas a significant decrease in the latter enzyme was noted in the abdominal segment of the dog. No gradient of activity was apparent in man. Liver exhibited the lowest activity for both enzymes in man, highest in the dog and intermediate in the rabbit. The above findings suggest a biologic species difference between the aorta of man, the rabbit and the dog, which may be partly ascribed to a difference in the components of the above two enzymatic systems. The same species difference holds true for hepatic tissue.

scholarly journals Redox-Modulating Agents in the Treatment of Viral Infections

2020 ◽  
Vol 21 (11) ◽  
pp. 4084 ◽  
Author(s):  
Paola Checconi ◽  
Marta De Angelis ◽  
Maria Elena Marcocci ◽  
Alessandra Fraternale ◽  
Mauro Magnani ◽  
...  
Keyword(s):  
Inflammatory Response ◽  
Redox State ◽  
Viral Infections ◽  
Rna Virus ◽  
Influenza Virus Infection ◽  
Redox Balance ◽  
Physiological Conditions ◽  
Cell Functions ◽  
Enzymatic Systems ◽  
Strong Inflammatory Response

Viruses use cell machinery to replicate their genome and produce viral proteins. For this reason, several intracellular factors, including the redox state, might directly or indirectly affect the progression and outcome of viral infection. In physiological conditions, the redox balance between oxidant and antioxidant species is maintained by enzymatic and non-enzymatic systems, and it finely regulates several cell functions. Different viruses break this equilibrium and induce an oxidative stress that in turn facilitates specific steps of the virus lifecycle and activates an inflammatory response. In this context, many studies highlighted the importance of redox-sensitive pathways as novel cell-based targets for therapies aimed at blocking both viral replication and virus-induced inflammation. In the review, we discuss the most recent findings in this field. In particular, we describe the effects of natural or synthetic redox-modulating molecules in inhibiting DNA or RNA virus replication as well as inflammatory pathways. The importance of the antioxidant transcription factor Nrf2 is also discussed. Most of the data reported here are on influenza virus infection. We believe that this approach could be usefully applied to fight other acute respiratory viral infections characterized by a strong inflammatory response, like COVID-19.

The hypolipidemic effect and antithrombotic activity of Mucuna pruriens protein hydrolysates

2016 ◽  
Vol 7 (1) ◽  
pp. 434-444 ◽  
Author(s):  
Francisco Herrera Chalé ◽  
Jorge Carlos Ruiz Ruiz ◽  
David Betancur Ancona ◽  
Juan José Acevedo Fernández ◽  
Maira Rubi Segura Campos
Keyword(s):  
Protein Hydrolysates ◽  
Mucuna Pruriens ◽  
Hypolipidemic Effect ◽  
Antithrombotic Activity ◽  
Protein Concentrates ◽  
Enzymatic Systems ◽  
Peptide Fractions

Hydrolysates and peptide fractions (PF) obtained fromM. pruriensprotein concentrates with commercial and digestive enzymatic systems were studied for their hypolipidemic and antithrombotic activities.

scholarly journals Structural studies on M. tuberculosis O6-methylguanine methyltransferase

2014 ◽  
Vol 70 (a1) ◽  
pp. C832-C832
Author(s):  
Menico Rizzi ◽  
Riccardo Miggiano ◽  
Samarpita Lahiri ◽  
Giuseppe Perugino ◽  
Maria Ciaramella ◽  
...  
Keyword(s):  
Excision Repair ◽  
Single Step ◽  
Double Stranded Dna ◽  
Nucleotide Excision ◽  
Enzymatic Systems ◽  
Methylguanine Methyltransferase ◽  
Mutagenic Effects ◽  
Wild Type Form

Mycobacterium tuberculosis (MTB) is an extremely well adapted human pathogen capable to survive for decades inside the hostile environment represented by the host's infected macrophages despite exposure to multiple potential DNA-damaging stresses. In order to maintain a remarkable low level of genetic diversity, MTB deploys different strategies of DNA repair, including multi-enzymatic systems, such as Nucleotide Excision Repair, and single-step repair. In particular, to counteract the mutagenic effects of DNA alkylation, MTB performs the direct alkylated-base reversal by sacrificing one molecule of a DNA-protein alkyltransferase, such as O6-methylguanine methyltransferase (OGT; orf: Rv1316c). We present here the biochemical and structural characterization of recombinant mycobacterial OGT (MtOGT) in its wild-type form along with its mutated variants mimicking the ones occurring in relevant clinical strains (i.e. MtOGT-T15S and MtOGT-R37L). Our studies reveal that MtOGT-R37L is severely impaired in its activity as consequence of its ten-fold lower affinity for modified double-stranded DNA (dsDNA) (1). Further investigations on a new structure-based panel of OGT versions, designed to explore different molecular environment at position 37, allowed us a better understanding of the functional role of the MtOGT Arg37-bearing loop during catalysis. Moreover, we solved the crystal structure of MtOGT in covalent complex with modified dsDNA that reveals an unprecedented MtOGT::DNA architecture, suggesting that the MtOGT monomer performing the catalysis needs assisting unreacted subunits during cooperative DNA binding. This work is supported by European Community FP7 program SYSTEMTB (Health-F4-2010-241587)

scholarly journals Oxygen-tolerant proton reduction catalysis: much O2 about nothing?

2015 ◽  
Vol 8 (8) ◽  
pp. 2283-2295 ◽  
Author(s):  
David W. Wakerley ◽  
Erwin Reisner
Keyword(s):  
Adverse Effects ◽  
Proton Reduction ◽  
Catalytic Surfaces ◽  
Enzymatic Systems

This perspective summarises strategies for avoiding adverse effects of O2 on H2-evolving enzymatic systems, molecular synthetic catalysts and catalytic surfaces.

Analysis of linoleic acid hydroperoxides generated by biomimetic and enzymatic systems through an integrated methodology

2011 ◽  
Vol 34 (3) ◽  
pp. 1474-1481 ◽  
Author(s):  
Juan José Villaverde ◽  
Sónia A.O. Santos ◽  
Mário M.Q. Simões ◽  
Carlos Pascoal Neto ◽  
M. Rosário M. Domingues ◽  
...  
Keyword(s):  
Linoleic Acid ◽  
Integrated Methodology ◽  
Enzymatic Systems
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