期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 77, 期 -, 页码 1251-1269出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798321009025
关键词
neutron protein crystallography; X-ray diffraction; metalloproteins; enzymatic mechanisms; protonation; radiation damage
资金
- National Research Foundation (NRF), South Africa
- Oak Ridge National Laboratory Graduate Opportunities (GO!) Program
- USDA NIFA Hatch [211001]
Metalloproteins catalyze reactions with enhanced chemical functionality due to their metal cofactor. However, radiation damage in structural studies can introduce artefacts complicating interpretation. Neutron protein crystallography remains the only probe leaving samples devoid of radiation damage.
Metalloproteins catalyze a range of reactions, with enhanced chemical functionality due to their metal cofactor. The reaction mechanisms of metalloproteins have been experimentally characterized by spectroscopy, macromolecular crystallography and cryo-electron microscopy. An important caveat in structural studies of metalloproteins remains the artefacts that can be introduced by radiation damage. Photoreduction, radiolysis and ionization deriving from the electromagnetic beam used to probe the structure complicate structural and mechanistic interpretation. Neutron protein diffraction remains the only structural probe that leaves protein samples devoid of radiation damage, even when data are collected at room temperature. Additionally, neutron protein crystallography provides information on the positions of light atoms such as hydrogen and deuterium, allowing the characterization of protonation states and hydrogen-bonding networks. Neutron protein crystallography has further been used in conjunction with experimental and computational techniques to gain insight into the structures and reaction mechanisms of several transition-state metal oxidoreductases with iron, copper and manganese cofactors. Here, the contribution of neutron protein crystallography towards elucidating the reaction mechanism of metalloproteins is reviewed.
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