| Structural highlights
4uwn is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , |
| Related: | 4uwu, 4uwv |
| Activity: | Lysozyme, with EC number 3.2.1.17 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1]
Publication Abstract from PubMed
A few ruthenium based metal carbonyl complexes, e.g. CORM-2 and CORM-3, have therapeutic activity attributed to their ability to deliver CO to biological targets. In this work, a series of related complexes with the formula [Ru(CO)3Cl2L] (L = DMSO (), l-H3CSO(CH2)2CH(NH2)CO2H) (); d,l-H3CSO(CH2)2CH(NH2)CO2H (); 3-NC5H4(CH2)2SO3Na (); 4-NC5H4(CH2)2SO3Na (); PTA (); DAPTA (); H3CS(CH2)2CH(OH)CO2H (); CNCMe2CO2Me (); CNCMeEtCO2Me (); CN(c-C3H4)CO2Et) ()) were designed, synthesized and studied. The effects of L on their stability, CO release profile, cytotoxicity and anti-inflammatory properties are described. The stability in aqueous solution depends on the nature of L as shown using HPLC and LC-MS studies. The isocyanide derivatives are the least stable complexes, and the S-bound methionine oxide derivative is the more stable one. The complexes do not release CO gas to the headspace, but release CO2 instead. X-ray diffraction of crystals of the model protein Hen Egg White Lysozyme soaked with () and () shows the addition of RuII(CO)(H2O)4 at the His15 binding site. Soakings with () produced the metallacarboxylate [Ru(COOH)(CO)(H2O)3]+ bound to the His15 site. The aqueous chemistry of these complexes is governed by the water-gas shift reaction initiated with the nucleophilic attack of HO- on coordinated CO. DFT calculations show this addition to be essentially barrierless. The complexes have low cytotoxicity and low hemolytic indices. Following i.v. administration of CORM-3, the in vivo bio-distribution of CO differs from that obtained with CO inhalation or with heme oxygenase stimulation. A mechanism for CO transport and delivery from these complexes is proposed.
A contribution to the rational design of Ru(CO)ClL complexes for in vivo delivery of CO.,Seixas JD, Santos MF, Mukhopadhyay A, Coelho AC, Reis PM, Veiros LF, Marques AR, Penacho N, Goncalves AM, Romao MJ, Bernardes GJ, Santos-Silva T, Romao CC Dalton Trans. 2014 Nov 27. PMID:25427784[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
- ↑ Seixas JD, Santos MF, Mukhopadhyay A, Coelho AC, Reis PM, Veiros LF, Marques AR, Penacho N, Goncalves AM, Romao MJ, Bernardes GJ, Santos-Silva T, Romao CC. A contribution to the rational design of Ru(CO)ClL complexes for in vivo delivery of CO. Dalton Trans. 2014 Nov 27. PMID:25427784 doi:http://dx.doi.org/10.1039/c4dt02966f
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