2fnw
From Proteopedia
Pseudomonas aeruginosa E2Q/H83Q/M109H-azurin RE(PHEN)(CO)3
Structural highlights
FunctionAZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase. Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe triplet metal-to-ligand charge transfer ((3)MLCT) dynamics of two structurally characterized Re(I)(CO)(3)(phen)(HisX)-modified (phen = 1,10-phenanthroline; X = 83, 109) Pseudomonas aeruginosa azurins have been investigated by picosecond time-resolved infrared (TRIR) spectroscopy in aqueous (D(2)O) solution. The (3)MLCT relaxation dynamics exhibited by the two Re(I)-azurins are very different from those of the sensitizer [Re(I)(CO)(3)(phen)(im)](+) (im = imidazole). Whereas the Re(I)(CO)(3) intramolecular vibrational relaxation in Re(I)(CO)(3)(phen)(HisX)Az (4 ps) is similar to that of [Re(I)(CO)(3)(phen)(im)](+) (2 ps), the medium relaxation is much slower ( approximately 250 vs 9.5 ps); the 250-ps relaxation is attributable to reorientation of D(2)O molecules as well as structural reorganization of the rhenium chromophore and nearby polar amino acids in each of the modified proteins. Excited-state dynamics of structurally characterized [ReI(CO)3(phen)(HisX)]+ (X = 83, 109) Pseudomonas aeruginosa azurins in aqueous solution.,Blanco-Rodriguez AM, Busby M, Gradinaru C, Crane BR, Di Bilio AJ, Matousek P, Towrie M, Leigh BS, Richards JH, Vlcek A Jr, Gray HB J Am Chem Soc. 2006 Apr 5;128(13):4365-70. PMID:16569013[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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