Results 31 to 40 of about 3,386 (219)
Label-free photoacoustic microscopy of cytochromes [PDF]
, 2013 Photoacoustic microscopy (PAM) has achieved submicron lateral resolution in showing subcellular structures; however, relatively few endogenous subcellular contrasts have so far been imaged. Given that the hemeprotein, mostly cytochromes in general cells,
Wang, Lihong V. +4 more
core +1 more source
The effects of nitroxyl (HNO) on soluble guanylate cyclase activity: interactions at ferrous heme and cysteine thiols [PDF]
, 2009 It has been previously proposed that nitric oxide (NO) is the only biologically relevant nitrogen oxide capable of activating the enzyme soluble guanylate cyclase (sGC). However, recent reports implicate HNO as another possible activator of sGC.
Adrian J. Hobbs +85 more
core +2 more sources
Design of Artificial Enzymes: Insights into Protein Scaffolds
ChemBioChem, Volume 24, Issue 6, March 14, 2023., 2023 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]
, 2011 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]
Journal of Inorganic Biochemistry, 2014 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
Factors Controlling the Reactivity of Hydrogen Sulfide with Hemeproteins [PDF]
Biochemistry, 2009 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
Murburn Concept: A Molecular Explanation for Hormetic and Idiosyncratic Dose Responses
Dose-Response, 2018 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
Cytochrome c signalosome in mitochondria [PDF]
, 2011 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
The Reactions of Antibodies with Hemeprotein Antigens
Journal of Biological Chemistry, 1969 Robert W. Noble +2 more
openalex +2 more sources
pH-dependent mechanism of nitric oxide release in nitrophorins 2 and 4 [PDF]
, 2009 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