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Services

 

Nanochemistry:

- Functionalization of nanotubes
- Organiic synthesis
- Polyelectrolytes
- TEM imaging

Environmental chemistry:

- Analysis of pollutants
- Purification methods
- Soil and water samples

 

Research Areas

- Toxicology
- Energy Sciences
- Pollution dynamics
- Water pollution circulation
- Life cycle of pollutants
- Heavy Metals
- Molecular interactions
- Environmental remediation
- Waste management
- Exotic Materials

 

 

Fjordforsk A.S. Midtun, 6894 Vangsnes, Norway.
Org.nr: 911659654 | www.fjordforsk.no

Natural bond orbital analysis of metalloenzyme complexes.

 

Project duration: 2015 -


Collaborating institute:

Protein Structure and Function Laboratory. University of Queensland. Brisbane Australia.

Research Centre for Infectious Diseases. School of Biological Sciences. The University of Adelaide. Adelaide. Australia.


Project description:

Natural Bond Orbital (NBO) analysis is one of the most powerful tools for understanding electron-electron interactions at a high resolution, where ionic, covalent and other interactions such as lone pair-based bond formation are studied and visualized in 3D, evaluated for their potential energy landscape and also for their spin distribution across several coordinating nuclei. The nature of enzyme-metal complexes proves as a valuable field of study for the derivation of NBO interpretations as several metal-binding complexes require high-precision basis sets for studying the electronic correlation and exchange occurring between the metal valence shell and the organic ligand atoms. With a combination of relativistic spin-orbit coupling, powerful quantum chemical software and high-performance computing hardware, the quantistic behavior of electrons at enzymes' catalytic metal-bound active sites is studied and enzyme mechanisms understood to greater detail. The impacts of the results are within the fields of enzymology, virology, cellular biology and protein engineering.

 

Project participants: Manzetti S. Kobe B, McDevitt C., O'Mara M.

 

Keywords: Structural biology, enzymology, quantum mechanics, active site, transition metals, natural bond orbitals, NBO, protein mechanics.

 

Fig. The 4d y² occupied orbital of Cadmium forming a weak bond with two Histidine residues from a key-metalloenzyme from the Staphylococcus strain, playing a central role in the differentiation with the native metal ion. Click to enlarge.

 

 

Publications:

Manzetti S. (2017). Quantum chemical calculations of the active site of the solute-binding protein PsaA from Streptococcus pneumoniae explain electronic selectivity of metal binding. Structural Chemistry, in press. DOI: 10.1007/s11224-017-1036-6

Manzetti S, Kobe B. (2015). Quantum chemical calculations of the active site of PsaA enzyme from Staphylococcus Pneumoniae reveal a crucial relationship between ionic electron configuration and enzyme activity. Annual meeting of the Swedish Chemical Society Theoretical Chemistry Section 2015. Book of Abstracts. August 25-27 2015 Kalmar, Sweden. STC2015. Download here.


 


Fjordforsk is a member of the American Chemical Society. Please visit the society following the logo below.

News

 

16 Jun.: Study on the atomic, electronic and material properties of MgO nanoparticles. Published in Material Chemistry and Physics.

10 Apr.: New study on semiconducting nanomaterials for spintronics and nanoelectronics published. Read more

27 Okt.: Review on biochemical effects from exhaust emissions published in Pathophysiology. Read more

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