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Changjian Feng
Researcher at University of New Mexico
Publications - 73
Citations - 1632
Changjian Feng is an academic researcher from University of New Mexico. The author has contributed to research in topics: Nitric oxide synthase & Heme. The author has an hindex of 21, co-authored 71 publications receiving 1523 citations. Previous affiliations of Changjian Feng include University of Queensland & Duke University.
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Sulfite oxidizing enzymes
TL;DR: Recent developments in the understanding of sulfite oxidizing enzyme mechanisms that are driven by a combination of molecular biology, rapid kinetics, pulsed electron paramagnetic resonance (EPR), and computational techniques are the subject of this review.
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Effect of solution viscosity on intramolecular electron transfer in sulfite oxidase.
TL;DR: Results are consistent with the role of conformational changes on IET in sulfite oxidase, which helps to clarify the inconsistency between the large rate constant for IET between the Mo and Fe centers and the long distance between these two metal centers observed in the crystal structure.
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Mechanism of nitric oxide synthase regulation: Electron transfer and interdomain interactions
TL;DR: An improved understanding of the role of interdomain FMN/heme interaction and CaM binding may serve as the basis for the design of new selective inhibitors of NOS isoforms.
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A voltammetric study of interdomain electron transfer within sulfite oxidase.
TL;DR: Protein film voltammetry of chicken liver sulfite oxidase (SO) bound at the pyrolytic graphite "edge" or modified gold electrodes shows that catalytic electron transport is controlled by the inherent electrochemical characteristics of the heme b domain and conformational changes that allow intramolecular electron transfer with the molybdenum active site.
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Pulsed EPR Determination of the Distance between Heme Iron and FMN Centers in a Human Inducible Nitric Oxide Synthase
TL;DR: The relaxation-induced dipolar modulation enhancement (RIDME) technique is used to measure the electron spin echo envelope modulation caused by the dipole interactions between paramagnetic FMN and heme iron centers in the FMNH(*): FMN semiquinone form of a human inducible NOS (iNOS) bidomain oxygenase/FMN construct.