Results 31 to 40 of about 3,392 (222)
Design of Artificial Enzymes: Insights into Protein Scaffolds
The design of artificial enzymes has emerged as a promising tool for the generation of potent biocatalysts able to promote new‐to‐nature reactions. This review aims to give a general overview of suitable protein scaffolds, that could be functionalized with an artificial moiety to develop versatile artificial catalysts. Abstract The design of artificial
Stefanie Hanreich +2 more
wiley +1 more source
Hydrogen Sulfide: Redox Metabolism and Signaling [PDF]
The recognition of hydrogen sulfide (H2S) as an endogenously produced gas with signaling potential has stimulated research on a multitude of physiological effects mediated in the cardiovascular, immune, gastrointestinal, genitourinary, endocrine, and ...
Banerjee, Ruma
core +1 more source
Hydrogen sulfide activation in hemeproteins: The sulfheme scenario [PDF]
Traditionally known as a toxic gas, hydrogen sulfide (H2S) is now recognized as an important biological molecule involved in numerous physiological functions. Like nitric oxide (NO) and carbon monoxide (CO), H2S is produced endogenously in tissues and cells and can modulate biological processes by acting on target proteins.
Bessie B, Ríos-González +3 more
openaire +2 more sources
Murburn Concept: A Molecular Explanation for Hormetic and Idiosyncratic Dose Responses
Recently, electron transfers and catalyses in a bevy of redox reactions mediated by hemeproteins were explained by murburn concept. The term “murburn” is abstracted from “ mur ed burn ing ” or “ m ild u n r estricted burn ing ” and connotes a novel “ m ...
Abhinav Parashar +2 more
doaj +1 more source
Factors Controlling the Reactivity of Hydrogen Sulfide with Hemeproteins [PDF]
Hemoglobin I (HbI) from the clam Lucina pectinata is an intriguing hemeprotein that binds and transports H(2)S to sulfide-oxidizing chemoautotrophic bacteria to maintain a symbiotic relationship and to protect the mollusk from H(2)S toxicity. Single point mutations at E7, B10, and E11 were introduced into the HbI heme pocket to define the reactivity of
Ruth, Pietri +9 more
openaire +2 more sources
Cytochrome c signalosome in mitochondria [PDF]
Cytochrome c delicately tilts the balance between cell life (respiration) and cell death (apoptosis). Whereas cell life is governed by transient electron transfer interactions of cytochrome c inside the mitochondria, the cytoplasmic adducts of cytochrome
Díaz Moreno, Irene +3 more
core +1 more source
Mechanism of Sulfide Binding by Ferric Hemeproteins
The reaction of hydrogen sulfide (H2S) with hemeproteins is a key physiological reaction; still, its mechanism and implications are not completely understood. In this work, we propose a combination of experimental and theoretical tools to shed light on the reaction in model system microperoxidase 11 (MP11-FeIII) and myoglobin (Mb-FeIII), from the ...
Fernando M. Boubeta +5 more
openaire +3 more sources
pH-dependent mechanism of nitric oxide release in nitrophorins 2 and 4 [PDF]
Nitrophorins are NO carrier proteins that transport and release NO through a pH-dependent conformational change. They bind NO tightly in a low pH environment and release it in a higher pH environment.
Estrin, Dario Ariel +5 more
core +1 more source
Characterization of a globin-coupled oxygen sensor with a gene-regulating function [PDF]
Globin-coupled sensors (GCSs) are multiple-domain transducers, consisting of a regulatory globin-like heme-binding domain and a linked transducer domain(s). GCSs have been described in both Archaea and bacteria. They are generally assumed to bind O2 (and
Alam, M +13 more
core +1 more source
Iron Metabolism: From Health to Disease [PDF]
Background Iron is vital for almost all living organisms by participating in a wide range of metabolic processes. However, iron concentration in body tissues must be tightly regulated since excessive iron may lead to microbial infections or cause tissue
Fernandes, Rúben +2 more
core +1 more source

