Results 111 to 120 of about 428,654 (353)

Resistance of Nitric Oxide Dioxygenase and Cytochrome c Oxidase to Inhibition by Nitric Oxide and Other Indications of the Spintronic Control of Electron Transfer

open access: yesBiophysica
Heme enzymes that bind and reduce O2 are susceptible to poisoning by NO. The high reactivity and affinity of NO for ferrous heme produces stable ferrous-NO complexes, which in theory should preclude O2 binding and turnover.
Paul R. Gardner
doaj   +1 more source

Importance of Val567 on heme environment and substrate recognition of neuronal nitric oxide synthase

open access: yesFEBS Open Bio, 2018
Nitric oxide (NO) produced by mammalian nitric oxide synthases (mNOSs) is an important mediator in a variety of physiological functions. Crystal structures of mNOSs have shown strong conservation of the active‐site residue Val567 (numbering for rat ...
Inger K. Olsbu   +4 more
doaj   +1 more source

Heme-binding by Drosophila retinoid- and fatty acid-binding glycoprotein (RFABG), a member of the proapolipophorin gene family

open access: yesJournal of Lipid Research, 1999
We previously have cloned and characterized a retinoid- and fatty acid-binding glycoprotein (RFABG) isolated from the heads of Drosophila melanogaster. The protein is composed of two glycosylated subunits (Mr = >200,000 and 70,000) and is a member of the
Todd Duncan   +4 more
doaj   +1 more source

Mutagenic and Spectroscopic Investigation of pH Dependent CooA DNA Binding [PDF]

open access: yes, 2017
The carbon monoxide (CO) sensing heme protein, CooA, is a transcription factor which exists in several bacteria that utilize CO as an energy source. CooA positively regulates the expression of coo genes in the presence of CO such that the corresponding ...
Weaver, Brian R.
core   +1 more source

The effects of nitroxyl (HNO) on soluble guanylate cyclase activity: interactions at ferrous heme and cysteine thiols [PDF]

open access: yes, 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

Unraveling the Role of Heme in Neurodegeneration

open access: yesFrontiers in Neuroscience, 2018
Heme (iron-protoporphyrin IX) is an essential co-factor involved in several biological processes, including neuronal survival and differentiation. Nevertheless, an excess of free-heme promotes oxidative stress and lipid peroxidation, thus leading to cell
D. Chiabrando   +3 more
semanticscholar   +1 more source

Dysfunctional TRIM31 of POMC Neurons Provokes Hypothalamic Injury and Peripheral Metabolic Disorder under Long‐Term Fine Particulate Matter Exposure

open access: yesAdvanced Science, EarlyView.
Particulate matter ≤2.5 µm (PM2.5) elevates risks of neurological and chronic metabolic diseases, but the underlying mechanisms linking PM2.5‐induced central nervous system (CNS) injury to metabolic dysfunction remain unclear. Hypothalamic pro‐opiomelanocortin‐expressing (POMC+) neurons regulate systemic metabolic homeostasis, and tripartite motif ...
Chenxu Ge   +21 more
wiley   +1 more source

Loss of the putative Rab GTPase, Ypt7, impairs the virulence of Cryptococcus neoformans

open access: yesFrontiers in Microbiology
Small GTPases of the Rab family coordinate multiple membrane fusion and trafficking events in eukaryotes. In fungi, the Rab GTPase, Ypt7, plays a critical role in late endosomal trafficking, and is required for homotypic fusion events in vacuole ...
Guanggan Hu   +11 more
doaj   +1 more source

Rotational cooling of molecules using lamps [PDF]

open access: yes, 2004
We investigate theoretically the application of tailored incoherent far-infrared fields in combination with laser excitation of a single rovibrational transition for rotational cooling of translationally cold polar diatomic molecules. The cooling schemes
Bethlem H   +10 more
core   +2 more sources

Mitochondrial CISD1 Modulates Microglial Metabolic Reprogramming to Drive Stress Susceptibility in Mice

open access: yesAdvanced Science, EarlyView.
CDGSH iron sulfur domain 1 (CISD1) mitigates oxidative stress by promoting NADH oxidation and Coenzyme Q (CoQ) reduction. Under chronic stress, elevated CISD1 expression in microglia enhances NAD⁺ production, thereby increasing GAPDH activity and glycolytic flux, while reducing ATP synthesis by inhibiting proton transfer from mitochondrial complexes I ...
Wanting Dong   +5 more
wiley   +1 more source

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