Cryocrystallography of metalloprotein reaction intermediates.
Freeze-trapping reaction intermediates in macromolecular crystals is now a proven technique for obtaining their high-resolution structures by X-ray crystallography. The structural study of metalloprotein mechanisms has spearheaded this work, mainly because of the increased availability of single-crystal UV/visible spectrophotometry that enables reaction monitoring in the crystalline state. In particular, through formation of the frozen glass state, the stabilization of intermediates involving dissolved gases has yielded some of the most spectacular results. Metalloprotein systems still dominate this field, and the most recent successes, along with the accompanying advances in methodology, are presented.
Wilmot
Carrie M
CM
Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, 6-155 Jackson Hall, 321 Church Street SE, Minneapolis, Minnnesota 55455, USA.
Pearson
Arwen R
AR
D003080:Cold Temperature; D003460:Crystallization; D018360:Crystallography, X-Ray; D003580:Cytochromes; D019951:DNA Polymerase beta / Q000737:chemistry; D003576:Electron Transport Complex IV / Q000737:chemistry; D008024:Ligands; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism; D009572:Nitrite Reductases / Q000737:chemistry
D003580:Cytochromes; D008024:Ligands; D008667:Metalloproteins; D009572:Nitrite Reductases; C028123:nitrite reductase (NO-forming); D003576:Electron Transport Complex IV; D019951:DNA Polymerase beta