Function of Mitochondrial Stat3 in Cellular Respiration
Data indicate that Stat3 is required for optimal function of the ETC, which may allow it to orchestrate responses to cellular homeostasis.
Release of reactive nitrogen intermediates and reactive oxygen intermediates from mouse peritoneal macrophages. Comparison of activating cytokines and evidence for independent production.
Testing as a sole agent, IFN-gamma was the only one of the 12 cytokines capable of inducing both NO2- and H2O2 release and the pathways leading to secretion of H2 O2 and No2- are independent.
Mammalian nitric oxide synthases.
Nitric oxide synthases: properties and catalytic mechanism.
Update on Mechanism and Catalytic Regulation in the NO Synthases*
- D. Stuehr, J. Santolini, Zhi‐qiang Wang, Chin-Chuan Wei, S. Adak
- Biology, ChemistryJournal of Biological Chemistry
- 27 August 2004
This minireview updates the NO biosynthetic mechanism and describes a global catalytic model that highlights the role of NO as an intrinsic regulator.
Nitric oxide. A macrophage product responsible for cytostasis and respiratory inhibition in tumor target cells
A metabolic pathway of activated macrophages (M phi) involving oxidation of the guanido nitrogens of L-arginine is required for inhibition of growth and respiration of some target cells. The goal of…
Structure of nitric oxide synthase oxygenase dimer with pterin and substrate.
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…
Structure-function aspects in the nitric oxide synthases.
- D. Stuehr
- BiologyAnnual Review of Pharmacology and Toxicology
This chapter summarizes information regarding the structure-function aspects of the NOSs, which includes composition of the domains, the protein residues and regions involved in prosthetic group binding, catalytic properties of the domain, the relationship between dimeric structure and prosthetic Group binding and function, and factors that control assembly of NOS in cells.
Structural Basis for Isozyme-specific Regulation of Electron Transfer in Nitric-oxide Synthase*[boxs]
This work addresses current questions regarding NOS activity and regulation by combining mutagenesis and biochemistry with crystal structure determination of a fully assembled, electron-supplying, neuronal NOS reductase dimer and structurally elucidate the unique mechanisms for isozyme-specific regulation of electron transfer in NOS.
Purification and characterization of the cytokine-induced macrophage nitric oxide synthase: an FAD- and FMN-containing flavoprotein.
- D. Stuehr, H. Cho, N. Kwon, M. Weise, C. Nathan
- BiologyProceedings of the National Academy of Sciences…
- 1 September 1991
Gel filtration chromatography indicated that the induced NO synthase was catalytically competent as a dimer of approximately 250 kDa but could be dissociated into inactive monomers of approximately 130 kDa in the absence of L-arginine, FAD, and tetrahydrobiopterin.