NADPH–cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family
NADPH–cytochrome P450 oxidoreductase (CYPOR) and nitric oxide synthase (NOS), two
members of the diflavin oxidoreductase family, are multi-domain enzymes containing distinct …
members of the diflavin oxidoreductase family, are multi-domain enzymes containing distinct …
Towards the free energy landscape for catalysis in mammalian nitric oxide synthases
NGH Leferink, S Hay, SEJ Rigby… - The FEBS …, 2015 - Wiley Online Library
The general requirement for conformational sampling in biological electron transfer
reactions catalysed by multi‐domain redox systems has been emphasized in recent years …
reactions catalysed by multi‐domain redox systems has been emphasized in recent years …
Nitric oxide synthase domain interfaces regulate electron transfer and calmodulin activation
Nitric oxide (NO) produced by NO synthase (NOS) participates in diverse physiological
processes such as vasodilation, neurotransmission, and the innate immune response …
processes such as vasodilation, neurotransmission, and the innate immune response …
Single-molecule spectroscopy reveals how calmodulin activates NO synthase by controlling its conformational fluctuation dynamics
Mechanisms that regulate the nitric oxide synthase enzymes (NOS) are of interest in biology
and medicine. Although NOS catalysis relies on domain motions, and is activated by …
and medicine. Although NOS catalysis relies on domain motions, and is activated by …
Effects of somatothermal far‐infrared ray on primary dysmenorrhea: a pilot study
YM Ke, MC Ou, CK Ho, YS Lin, HY Liu… - Evidence‐Based …, 2012 - Wiley Online Library
The purpose of this study was to assess the beneficial effects of using a far‐infrared (FIR)
belt on the management of patients with primary dysmenorrhea. This is the first study to …
belt on the management of patients with primary dysmenorrhea. This is the first study to …
Endothelial nitric oxide synthase is regulated by ERK phosphorylation at Ser602
JC Salerno, DK Ghosh, R Razdan, KA Helms… - Bioscience …, 2014 - portlandpress.com
eNOS (endothelial nitric oxide synthase) contains a MAPK (mitogen-activated protein
kinase)-binding site associated with a major eNOS control element. Purified ERK …
kinase)-binding site associated with a major eNOS control element. Purified ERK …
[HTML][HTML] Calmodulin activates neuronal nitric oxide synthase by enabling transitions between conformational states
We recently showed that inducible nitric oxide synthase conformational intermediates can
be resolved via FMN fluorescence lifetimes. Here we show that neuronal NOS activation by …
be resolved via FMN fluorescence lifetimes. Here we show that neuronal NOS activation by …
Distinct conformational behaviors of four mammalian dual‐flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide …
Multidomain enzymes often rely on large conformational motions to function. However, the
conformational setpoints, rates of domain motions and relationships between these …
conformational setpoints, rates of domain motions and relationships between these …
Pulsed electron paramagnetic resonance study of domain docking in neuronal nitric oxide synthase: the calmodulin and output state perspective
AV Astashkin, L Chen, X Zhou, H Li… - The Journal of …, 2014 - ACS Publications
The binding of calmodulin (CaM) to neuronal nitric oxide synthase (nNOS) enables
formation of the output state of nNOS for nitric oxide production. Essential to NOS function is …
formation of the output state of nNOS for nitric oxide production. Essential to NOS function is …
Phosphorylation controls endothelial nitric-oxide synthase by regulating its conformational dynamics
The activity of endothelial NO synthase (eNOS) is triggered by calmodulin (CaM) binding
and is often further regulated by phosphorylation at several positions in the enzyme …
and is often further regulated by phosphorylation at several positions in the enzyme …