3RGS

Structural and kinetic analysis of the beef liver catalase with the ammonia as a ligand

Summary for 3RGS

• Entry DOI: 10.2210/pdb3rgs/pdb
• Related: 3RE8 3RGP
• Descriptor: Catalase, PROTOPORPHYRIN IX CONTAINING FE, AMMONIA, ... (4 entities in total)
• Functional Keywords: heme protein, oxidoreducatase, nh3 binding, oxidoreductase
• Biological source: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• Cellular location: Peroxisome: P00432
• Total number of polymer chains: 4
• Total formula weight: 230044.60

Authors

Purwar, N.,Schmidt, M. (deposition date: 2011-04-08, release date: 2011-05-11, Last modification date: 2023-09-13)

Primary citation

Purwar, N.,McGarry, J.M.,Kostera, J.,Pacheco, A.A.,Schmidt, M.
Interaction of nitric oxide with catalase: structural and kinetic analysis.
Biochemistry, 50:4491-4503, 2011

PubMed Abstract: We present the structures of bovine catalase in its native form and complexed with ammonia and nitric oxide, obtained by X-ray crystallography. Using the NO generator 1-(N,N-diethylamino)diazen-1-ium-1,2-diolate, we were able to generate sufficiently high NO concentrations within the catalase crystals that substantial occupation was observed despite a high dissociation rate. Nitric oxide seems to be slightly bent from the heme normal that may indicate some iron(II) character in the formally ferric catalase. Microspectrophotometric investigations inline with the synchrotron X-ray beam reveal photoreduction of the central heme iron. In the cases of the native and ammonia-complexed catalase, reduction is accompanied by a relaxation phase. This is likely not the case for the catalase NO complex. The kinetics of binding of NO to catalase were investigated using NO photolyzed from N,N'-bis(carboxymethyl)-N,N'-dinitroso-p-phenylenediamine using an assay that combines catalase with myoglobin binding kinetics. The off rate is 1.5 s(-1). Implications for catalase function are discussed.

PubMed: 21524057
DOI: 10.1021/bi200130r

Experimental method

X-RAY DIFFRACTION (1.99 Å)