2JI1

X-ray structure of wild-type superoxide reductase from Desulfoarculus baarsii

Summary for 2JI1

• Entry DOI: 10.2210/pdb2ji1/pdb
• Related: 1VZG 1VZH 1VZI 2JI2 2JI3
• Descriptor: Desulfoferrodoxin, FE (III) ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, raman spectroscopy, superoxide reductase, intermediate trapping, microspectrophotometry, detoxification, electron transport, iron, transport, redox states, metal-binding
• Biological source: Desulfarculus baarsii
• Total number of polymer chains: 4
• Total formula weight: 57312.66

Authors

Katona, G.,Carpentier, P.,Niviere, V.,Amara, P.,Adam, V.,Ohana, J.,Tsanov, N.,Bourgeois, D. (deposition date: 2007-02-24, release date: 2007-05-01, Last modification date: 2023-12-13)

Primary citation

Katona, G.,Carpentier, P.,Niviere, V.,Amara, P.,Adam, V.,Ohana, J.,Tsanov, N.,Bourgeois, D.
Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.
Science, 316:449-453, 2007

PubMed Abstract: Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (SOR), a nonheme mononuclear iron enzyme that scavenges superoxide radicals. X-ray diffraction data at 1.95 angstrom resolution and Raman spectra recorded in crystallo revealed iron-(hydro)peroxo intermediates with the (hydro)peroxo group bound end-on. The dynamic SOR active site promotes the formation of transient hydrogen bond networks, which presumably assist the cleavage of the iron-oxygen bond in order to release the reaction product, hydrogen peroxide.

PubMed: 17446401
DOI: 10.1126/science.1138885

Experimental method

X-RAY DIFFRACTION (1.7 Å)