C
Chaoqun Wu
Researcher at Cleveland Clinic
Publications - 15
Citations - 1839
Chaoqun Wu is an academic researcher from Cleveland Clinic. The author has contributed to research in topics: Heme & Nitric oxide synthase. The author has an hindex of 10, co-authored 10 publications receiving 1809 citations. Previous affiliations of Chaoqun Wu include Cleveland Clinic Lerner Research Institute & Scripps Research Institute.
Papers
More filters
Journal ArticleDOI
Structure of nitric oxide synthase oxygenase dimer with pterin and substrate.
Brian R. Crane,Brian R. Crane,Andrew S. Arvai,Dipak K. Ghosh,Chaoqun Wu,Elizabeth D. Getzoff,Dennis J. Stuehr,John A. Tainer +7 more
TL;DR: Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, the substrate L-arginine (L-Arg), or product analog thiocitrulline reveal how dimerization, cofactor tetrahydrobiopterin, and L-Arg binding complete the catalytic center for synthesis of the essential biological signal and cytotoxin nitricoxide.
Journal ArticleDOI
The structure of nitric oxide synthase oxygenase domain and inhibitor complexes.
Brian R. Crane,Andrew S. Arvai,Ratan Gachhui,Chaoqun Wu,Dipak K. Ghosh,Elizabeth D. Getzoff,Dennis J. Stuehr,John A. Tainer +7 more
TL;DR: Juxtaposed hydrophobic O2- and polar L-arginine-binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors and imply substrate-assisted catalysis.
Journal ArticleDOI
Interaction between Caveolin-1 and the Reductase Domain of Endothelial Nitric-oxide Synthase CONSEQUENCES FOR CATALYSIS
TL;DR: It is proposed that cav-1 binding to eNOS reductase compromises its ability to bind CaM and to donate electrons to the eN OS heme, thereby inhibiting NO synthesis.
Journal ArticleDOI
Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction.
Dipak K. Ghosh,Chaoqun Wu,Eva Pitters,Michael Moloney,Ernst R. Werner,Bernd Mayer,Dennis J. Stuehr +6 more
TL;DR: Results suggest that residues 66-114 of iNOSox are involved in productive H4biopterin interaction and subunit dimerization, and appears to stabilize the protein structure in this region, and through doing so activates iN OS for NO synthesis.
Journal ArticleDOI
Comparative Functioning of Dihydro- and Tetrahydropterins in Supporting Electron Transfer, Catalysis, and Subunit Dimerization in Inducible Nitric Oxide Synthase†
Anthony Presta,U. Siddhanta,Chaoqun Wu,Nicolas Sennequier,Liuxin Huang,Husam M. Abu-Soud,Serpil C. Erzurum,Dennis J. Stuehr +7 more
TL;DR: In this paper, pterin-free inducible NOS (iNOS) and iNOS reconstituted with eight different tetrahydro- or dihydropterins were investigated.