Results 51 to 60 of about 2,121 (177)
Protein Science, Volume 33, Issue 12, December 2024.Abstract Post‐translational modifications (PTMs) of proteins are ubiquitous processes present in all life kingdoms, involved in the regulation of protein stability, subcellular location and activity. In this context, cytochrome c (Cc) is an excellent case study to analyze the structural and functional changes induced by PTMS as Cc is a small ...
Joaquin Tamargo‐Azpilicueta +7 more
wiley +1 more source
, 2013 Several factors involved in the core circadian rhythm are PAS domain proteins, one of which, neuronal PAS2 (NPAS2), contains a heme-binding motif. It is thought that heme controls the transcriptional activity of core circadian factors BMAL1-NPAS2, and ...
Itoh, Ryuhei +6 more
core +1 more source
Access and Binding of H2S to Hemeproteins: The Case of HbI of Lucina pectinata [PDF]
, 2016 Hydrogen sulfide (H2S) was recently discovered as a gasotransmitter, capable of coordinating to the heme iron of hemeproteins. H2S is unique for its ability to render varying concentrations of the nucleophilic conjugate bases (HS- or S2-), either as free
Boechi, Leonardo +3 more
core +1 more source
Binding mechanism of disulfide species to ferric hemeproteins: The case of metmyoglobin
, 2023 The interactions of the heme iron of hemeproteins with sulfide and disulfide compounds are of potential interest as physiological signaling processes. While the interaction with hydrogen sulfide has been described computationally and experimentally, the ...
Estrin, Dario Ariel +9 more
core +1 more source
Access and Binding of H2S to Hemeproteins: The Case of HbI of Lucina pectinata
, 2016 Hydrogen sulfide (H2S) was recently discovered as a gasotransmitter, capable of coordinating to the heme iron of hemeproteins. H2S is unique for its ability to render varying concentrations of the nucleophilic conjugate bases (HS– or S2–), either as free
Dario A. Estrin (120783) +3 more
core +2 more sources
Role of the Circadian Gas-Responsive Hemeprotein NPAS2 in Physiology and Pathology
Biology, 2023 Neuronal PAS domain protein 2 (NPAS2) is a hemeprotein comprising a basic helix–loop–helix domain (bHLH) and two heme-binding sites, the PAS-A and PAS-B domains. This protein acts as a pyridine nucleotide-dependent and gas-responsive CO-dependent transcription factor and is encoded by a gene whose expression fluctuates with circadian rhythmicity. NPAS2
Emanuele Murgo +4 more
openaire +5 more sources
Chemistry – A European Journal, Volume 30, Issue 43, August 1, 2024.Porphyrin atropisomerism opens an entirely new toolbox, allowing for the precise design of a porphyrin's molecular shape. This review details how this phenomenon has been utilised across all fields of chemistry, focusing on molecular recognition, medicinal chemistry and catalysis.
Sophie Maguire +5 more
wiley +1 more source
The flavohemoglobin Yhb1 is a new interacting partner of the heme transporter Str3
Molecular Microbiology, Volume 122, Issue 1, Page 29-49, July 2024.A new mechanism for Yhb1 (orange) heme‐dependent activation involves direct interaction with the cell‐surface heme transporter Str3 (blue) in the presence of exogenous heme (red). Upon exposure to nitric oxide (˙NO), the expression of yhb1+ is induced, as its promoter is liberated from Fep1 repression (violet).
Florie Lo Ying Ping +4 more
wiley +1 more source
, 2017 It is challenging to develop a robust nanoprobe for real-time operational and accurate detection of heavy metals in single cells. Fe-CN coordination chemistry has been well studied to determine the structural characteristics of hemeproteins by different ...
Sumaira Hanif (3723790) +10 more
core +1 more source
Expanding the Catalytic Repertoire of Hemeproteins as Carbene Transferases to Access Diverse Molecular Structures [PDF]
, 2020 The efficiency, selectivity, and sustainability benefits offered by enzymes are enticing chemists to consider biocatalytic transformations to complement or even supplant more traditional synthetic routes.
Chen, Kai
core +1 more source