3re8

Structural and Kinetic Analysis of the Beef liver Catalase interacting with Nitric Oxide

spinqualitylabelsall models 3re8, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3re8 is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM Related: 3rgp, 3rgs Activity: Catalase, with EC number 1.11.1.6 Resources: FirstGlance, OCA, RCSB, PDBsum Function [CATA_BOVIN] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells. Publication Abstract from PubMed 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. Interaction of Nitric Oxide with Catalase: Structural and Kinetic Analysis.,Purwar N, McGarry JM, Kostera J, Pacheco AA, Schmidt M Biochemistry. 2011 May 6. PMID:21524057 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catalase

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