The scientist’s investigation covers issues in Stereochemistry, Heme, Cytochrome, Biochemistry and Protein structure. The various areas that Huiying Li examines in his Stereochemistry study include Nitric oxide synthase, Oxidoreductase, Active site, Cytochrome P450 and Binding site. His Nitric oxide synthase study improves the overall literature in Nitric oxide.
His research investigates the connection with Heme and areas like Flavin mononucleotide which intersect with concerns in Flavodoxin and Flavin adenine dinucleotide. His study in Cytochrome is interdisciplinary in nature, drawing from both Sorangium cellulosum, Epothilones, Thiazole and Flavin group. The concepts of his Protein structure study are interwoven with issues in Crystallography, Electron transport chain and Hydrogen bond.
His primary scientific interests are in Stereochemistry, Heme, Biochemistry, Nitric oxide synthase and Active site. His Stereochemistry research is multidisciplinary, relying on both Oxidoreductase, Protein structure, Cytochrome, Structure–activity relationship and Binding site. His Protein structure research includes elements of Electron transport chain and Hydrogen bond.
His research integrates issues of Crystallography, Ligand, Peroxidase, Cytochrome P450 and Tetrahydrobiopterin in his study of Heme. His Nitric oxide synthase study which covers Enzyme inhibitor that intersects with Molecular model. His Active site research incorporates themes from Biliverdin, Mutant and Pyrrolidine.
Biochemistry, Nitric oxide synthase, Heme, Enos and Stereochemistry are his primary areas of study. His Nitric oxide synthase research incorporates elements of Amino acid and Active site. He interconnects Photochemistry, Hydrogen bond and Tetrahydrobiopterin in the investigation of issues within Heme.
His research investigates the link between Enos and topics such as Propionate that cross with problems in Ligand and Pyrrolidine. His Stereochemistry study combines topics from a wide range of disciplines, such as Selectivity and Cytochrome. His research in Endothelial NOS intersects with topics in Protein structure and Binding site.
His primary areas of investigation include Endothelial NOS, Nitric oxide synthase, Biochemistry, Enzyme and Nitric oxide. Huiying Li combines topics linked to Active site with his work on Endothelial NOS. His work deals with themes such as Binding site and Staphylococcus aureus, which intersect with Nitric oxide synthase.
His work carried out in the field of Nitric oxide brings together such families of science as Dipole, Docking and Heme. His Heme research integrates issues from Biophysics, Spin label and Calmodulin. His studies in Oxidoreductase integrate themes in fields like Protein structure, Selectivity and Stereochemistry.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center.
C.S Raman;Huiying Li;Pavel Martásek;Vladimir Král.
Cell (1998)
The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
Huiying Li;Thomas L. Poulos.
Nature Structural & Molecular Biology (1997)
Structure of a cytochrome P450-redox partner electron-transfer complex.
Irina F. Sevrioukova;Huiying Li;Hong Zhang;Julian A. Peterson.
Proceedings of the National Academy of Sciences of the United States of America (1999)
Structure-function studies on nitric oxide synthases.
Huiying Li;Thomas L. Poulos.
Journal of Inorganic Biochemistry (2005)
Understanding the Role of the Essential Asp251 in Cytochrome P450cam Using Site-Directed Mutagenesis, Crystallography, and Kinetic Solvent Isotope Effect†
Momcilo Vidakovic;Stephen G. Sligar;Huiying Li;Thomas L. Poulos.
Biochemistry (1998)
Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase.
Huiying Li;C.S. Raman;Charles B. Glaser;Eric Blasko.
Journal of Biological Chemistry (1999)
The role of Thr268 in oxygen activation of cytochrome P450BM-3.
Hyeyeong Yeom;Stephen G. Sligar;Huiying Li;Thomas L. Poulos.
Biochemistry (1995)
The Novel Binding Mode of N-Alkyl-N'-Hydroxyguanidine to Neuronal Nitric Oxide Synthase Provides Mechanistic Insights into NO Biosynthesis
Huiying Li;Hideaki Shimizu;Mack Flinspach;Joumana Jamal.
Biochemistry (2002)
High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase
Christopher A. Bonagura;B. Bhaskar;Hideaki Shimizu;Huiying Li.
Biochemistry (2003)
Structural Basis for Effector Control and Redox Partner Recognition in Cytochrome P450
Sarvind Tripathi;Huiying Li;Thomas L. Poulos.
Science (2013)
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Publications: 23
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