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Cloning, expression, and characterization of a nitric oxide synthase protein from Deinococcus radiodurans
- Source :
- Proceedings of the National Academy of Sciences. 99:107-112
- Publication Year :
- 2001
- Publisher :
- Proceedings of the National Academy of Sciences, 2001.
-
Abstract
- We cloned, expressed, and characterized a hemeprotein from Deinococcus radiodurans ( D. radiodurans NO synthase, deiNOS) whose sequence is 34% identical to the oxygenase domain of mammalian NO synthases (NOSoxys). deiNOS was dimeric, bound substrate Arg and cofactor tetrahydrobiopterin, and had a normal heme environment, despite its missing N-terminal structures that in NOSoxy bind Zn 2+ and tetrahydrobiopterin and help form an active dimer. The deiNOS heme accepted electrons from a mammalian NOS reductase and generated NO at rates that met or exceeded NOSoxy. Activity required bound tetrahydrobiopterin or tetrahydrofolate and was linked to formation and disappearance of a typical heme-dioxy catalytic intermediate. Thus, bacterial NOS-like proteins are surprisingly similar to mammalian NOSs and broaden our perspective of NO biochemistry and function.
- Subjects :
- inorganic chemicals
Models, Molecular
Time Factors
Hemeprotein
Protein Conformation
Molecular Sequence Data
Electrons
Heme
Arginine
Ligands
Nitric Oxide
Catalysis
Cofactor
chemistry.chemical_compound
Protein structure
medicine
Animals
Amino Acid Sequence
Cloning, Molecular
Thermus
Peptide sequence
Multidisciplinary
Dose-Response Relationship, Drug
Sequence Homology, Amino Acid
biology
Deinococcus radiodurans
Hydrogen Peroxide
Tetrahydrobiopterin
Biological Sciences
biology.organism_classification
Biopterin
Molecular biology
Protein Structure, Tertiary
Nitric oxide synthase
Dithiothreitol
Kinetics
Zinc
Models, Chemical
chemistry
Biochemistry
biology.protein
Citrulline
Nitric Oxide Synthase
Dimerization
Oxidation-Reduction
NADP
Protein Binding
medicine.drug
Subjects
Details
- ISSN :
- 10916490 and 00278424
- Volume :
- 99
- Database :
- OpenAIRE
- Journal :
- Proceedings of the National Academy of Sciences
- Accession number :
- edsair.doi.dedup.....fc79e8d46a9b6827bf2ef74991c62892