Article
The C331A mutant of neuronal nitric-oxide synthase is defective in arginine binding.
The Journal of biological chemistry - 25 Dec 1998
Martásek P, Miller R T, Liu Q, Roman L J, Salerno J C, Migita C T, Raman C S, Gross S S, Ikeda-Saito M, Masters B S
Abstract excerpt
It has been proposed that Cys99 of human endothelial nitric oxide synthase (eNOS) is responsible for tetrahydrobiopterin (BH4) binding. To examine this possibility rigorously, we expressed rat neuronal NOS (nNOS) in Escherichia coli, with the homologous Cys331 to Ala mutation, and characterized s...
Topics
- Animals
- Arginine
- Biopterins
- Calmodulin
- Carbon Monoxide
- Catalytic Domain
- Conserved Sequence
- Cysteine
- Electron Spin Resonance Spectroscopy
- Escherichia coli
- Heme
- Mutation
- NADP
- Neurons
- Nitric Oxide Synthase
- Nitric Oxide Synthase Type I
- Oxidation-Reduction
- Rats