Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography. Issue 10 (4th October 2021)

• Record Type: Journal Article
• Authors: Schröder, Gabriela C.; Meilleur, Flora
• Is Part Of: Acta crystallographica. Volume 77:Issue 10(2021)
• Page Start: 1251
• Page End: 1269
• Publication Date: 2021-10-04
• Subjects: neutron protein crystallography -- X‐ray diffraction -- metalloproteins -- enzymatic mechanisms -- protonation -- radiation damage; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; Molecular biology -- Periodicals; Molecular structure -- Periodicals; Biomolecules -- Structure -- Periodicals; Cytology -- Periodicals; Biomolecules -- Structure; Crystallography; Cytology; Molecular biology; Molecular structure; X-ray crystallography; Periodicals; 548
• DOI: 10.1107/S2059798321009025
• Languages: English
• ISSNs: 2059-7983

Abstract

Abstract : Neutron protein crystallography provides insight into the structure and reaction mechanism of transition‐state metal oxidoreductases without resulting in radiation‐damage‐induced artefacts. Abstract : 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.