Limei Zhang

ORCID: 0000-0001-6807-5103
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About
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Research Areas
  • Trace Elements in Health
  • Metalloenzymes and iron-sulfur proteins
  • Electrochemical Analysis and Applications
  • RNA and protein synthesis mechanisms
  • Advanced biosensing and bioanalysis techniques
  • Ammonia Synthesis and Nitrogen Reduction
  • Microbial Fuel Cells and Bioremediation
  • Tuberculosis Research and Epidemiology
  • Drug Transport and Resistance Mechanisms
  • Metal complexes synthesis and properties
  • Metal-Catalyzed Oxygenation Mechanisms
  • Machine Learning in Bioinformatics
  • Protein Structure and Dynamics
  • Advanced battery technologies research
  • Innovative Teaching Methods
  • Fractal and DNA sequence analysis
  • Ion channel regulation and function
  • CRISPR and Genetic Engineering
  • Nicotinic Acetylcholine Receptors Study
  • Heavy Metal Exposure and Toxicity
  • RNA modifications and cancer
  • Biosensors and Analytical Detection
  • Hydrogen Storage and Materials
  • Bacterial Genetics and Biotechnology
  • Iron Metabolism and Disorders

Sun Yat-sen University
2024-2025

The First Affiliated Hospital, Sun Yat-sen University
2024-2025

Yunnan Agricultural University
2024

University of Nebraska–Lincoln
2018-2024

Chongqing Medical and Pharmaceutical College
2024

Chongqing Medical University
2024

First Affiliated Hospital of Sichuan Medical University
2023

Affiliated Hospital of Southwest Medical University
2022-2023

Fujian Agriculture and Forestry University
2022

Chinese Academy of Medical Sciences & Peking Union Medical College
2021

The identity of the interstitial light atom in center FeMo cofactor nitrogenase has been enigmatic since its discovery. Atomic-resolution x-ray diffraction data and an electron spin echo envelope modulation (ESEEM) analysis now provide direct evidence that ligand is a carbon species.

10.1126/science.1214025 article EN Science 2011-11-17

The ability of certain transition metals to mediate the reduction N2 NH3 has attracted broad interest in biological and inorganic chemistry communities. Early such as Mo W readily bind its protonation at one or more N atoms furnish M(NxHy) species that can be characterized and, turn, extrude NH3. By contrast, direct Fe–N2 Fe(NxHy) products been elusive. Herein, we show addition acid low temperature [(TPB)Fe(N2)][Na(12-crown-4)] results a new S = 1/2 Fe species. EPR, ENDOR, Mössbauer, EXAFS...

10.1021/jacs.5b03432 article EN Journal of the American Chemical Society 2015-05-22

Abstract The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the largest known metal cluster and catalyses 6-electron reduction dinitrogen to ammonium in biological nitrogen fixation. Only recently its atomic structure was clarified, while reactivity electronic remain under debate. Here we show that for resting S =3/2 state common iron oxidation assignments must be reconsidered. By a spatially resolved refinement anomalous scattering contributions 7 Fe atoms FeMoco,...

10.1038/ncomms10902 article EN cc-by Nature Communications 2016-03-14

Virtually all chemical bonds consist of one or several pairs electrons shared by two atoms. Examples σ-bonds made a single electron delocalized over neighboring atoms were until recently found only in gas-phase cations such as H2(+) and Li2(+) highly unstable species generated solid matrices. Only the past decade was bona fide one-electron bonding observed for molecules fluid solution. Here we report isolation structural characterization thermally stable compound featuring Cu-B bond, well...

10.1021/ja4006578 article EN Journal of the American Chemical Society 2013-02-19

Wilson's disease is a human genetic disorder which results in copper accumulation liver and brain. Treatments such as chelation therapy or dietary supplementation with zinc can ameliorate the effects of disease, but if left untreated, it hepatitis, neurological complications, death. Tetrathiomolybdate (TTM) promising new treatment for has been demonstrated both an animal model clinical trials. X-ray absorption spectroscopy suggests that TTM acts novel chelator, forming complex accumulated...

10.1021/bi801926e article EN Biochemistry 2009-01-15

ABSTRACT A multi‐vitamin auxotrophic Torulopsis glabrata strain, a pyruvate producer, was further engineered to produce fumaric acid. Using the genome‐scale metabolic model i NX804 of T. , four acid biosynthetic pathways, involving cytosolic enzymes, argininosuccinate lyase (ASL), adenylosuccinate (ADSL), fumarylacetoacetase (FAA), and fumarase (FUM1), were found. Athough single overexpression each enzymes in cytosol improved production, highest titer (5.62 g L −1 ) obtained with strain...

10.1002/bit.25334 article EN Biotechnology and Bioengineering 2014-07-24

In the nitrogenase molybdenum-iron (MoFe) protein, we have identified five potential substrate access pathways from protein surface to FeMo-cofactor (the active site) or P-cluster using experimental structures of Xe pressurized into MoFe crystals Azotobacter vinelandii and Clostridium pasteurianum. Additionally, all published including those Klebsiella pneumoniae, were analyzed for presence nonwater, small molecules bound interior. Each pathway is based on identification plausible routes...

10.1021/bi501313k article EN publisher-specific-oa Biochemistry 2015-02-24

This study explores the implementation and evaluation of online offline blended teaching model in Clinical Laboratory Hematology (CLH) laboratory course at Chengdu Medical College. To this end, 90 students majoring medical technology 2020 were selected as research subjects randomly divided into experimental control groups. The group adopted an model, while a traditional one. After-class tests, examinations, questionnaire surveys, student interviews conducted to evaluate effectiveness....

10.3389/feduc.2025.1497477 article EN cc-by Frontiers in Education 2025-02-03

The Cu(I) sensor Mycobacterium tuberculosis CsoR is a founding member of new metalloregulatory protein family. Here we show that two "atom" substitutions the Nε2 face coordinating histisine-61 allosterically uncouple and DNA binding, with no effect on binding affinity coordination structure. A model analogous to allosteric switch mechanism in Staphylococcus aureus CzrA, zinc completely different fold, proposed.

10.1021/ja908372b article EN Journal of the American Chemical Society 2009-11-24

Protein tyrosine O-sulfation (PTS) plays a crucial role in extracellular biomolecular interactions that dictate various cellular processes. It also involves the development of many human diseases. Regardless recent progress, our current understanding PTS is still its infancy. To promote and facilitate relevant studies, generally applicable method needed to enable efficient expression sulfoproteins with defined sulfation sites live mammalian cells. Here we report engineering, vitro...

10.1038/s41467-020-18629-9 article EN cc-by Nature Communications 2020-09-24

Drosophila melanogaster MTF-1 (dMTF-1) is a copper-responsive transcriptional activator that mediates resistance to Cu, as well Zn and Cd. Here, we characterize novel cysteine-rich domain which crucial for sensing excess intracellular copper by dMTF-1. Transgenic flies expressing mutant dMTF-1 containing alanine substitutions of two, four or six cysteine residues within the sequence (547)CNCTNCKCDQTKSCHGGDC(565) are significantly completely impaired in their ability protect from toxicity...

10.1093/nar/gkn103 article EN cc-by-nc Nucleic Acids Research 2008-04-13

Another iron in the fire: X-ray anomalous diffraction studies on nitrogenase MoFe protein show presence of a mononuclear site, designated as Fe16, which was previously identified either Ca2+ or Mg2+. The position absorption edge indicates that this site is oxidation state +2. high sequence conservation residues coordinated to Fe16 emphasizes potential importance nitrogenase. molybdenum–iron (MoFe) contains two types metalloclusters, [8Fe:7S] P-cluster and [7Fe:9S:Mo:C:homocitrate] FeMo...

10.1002/anie.201303877 article EN other-oa Angewandte Chemie International Edition 2013-08-21

The X-ray crystal structure of the nitrogenase MoFe protein from Clostridium pasteurianum (Cp1) has been determined at 1.08 Å resolution by multiwavelength anomalous diffraction phasing. Cp1 and ortholog Azotobacter vinelandii (Av1) represent two distinct families nitrogenases, differing primarily a long insertion in α-subunit deletion β-subunit relative to Av1. Comparison these structures atomic reveals conserved structural arrangements that are significant function nitrogenase. FeMo...

10.1107/s1399004714025243 article EN cc-by Acta Crystallographica Section D Biological Crystallography 2015-01-22

Yeast Cox4 is a zinc binding subunit of cytochrome c oxidase. the only cofactor-containing that not directly part catalytic core enzyme located in mitochondrial inner membrane. The Zn(II) site shown to be distinct from bovine ortholog, as it results x-ray structure entire oxidase having single histidyl residue and three conserved cysteines residues coordination sphere. Substitutions at Cys ligand positions result non-functional proteins fail lead assembly. Limited function exists His-119...

10.1074/jbc.m610303200 article EN cc-by Journal of Biological Chemistry 2007-01-11

We report a structural characterization of the molybdenum site recombinant Escherichia coli trimethylamine N-oxide (TMAO) reductase using X-ray absorption spectroscopy. The enzyme active shows considerable similarity to that dimethyl sulfoxide (DMSO) reductase, in that, like DMSO TMAO can exist multiple forms. Examination published crystal structure oxidase from Shewanella massilia indicates postulated Mo coordination is chemically impossible. presence structures provides potential...

10.1021/ic701956f article EN Inorganic Chemistry 2007-12-29
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