| FEBS Letters | |
| The critical role of tryptophan‐116 in the catalytic cycle of dimethylsulfoxide reductase from Rhodobacter capsulatus | |
| McEwan, Alastair G2  Ridge, Justin P2  Aguey-Zinsou, Kondo-Francois3  Bernhardt, Paul V3  Hanson, Graeme R1  | |
| [1] Centre for Magnetic Resonance, University of Queensland, Brisbane, Qld. 4072, Australia;Centre for Metals in Biology, School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Qld. 4072, Australia;Department of Chemistry, School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Qld. 4072, Australia | |
| 关键词: Dimethylsulfoxide reductase; Molybdenum enzyme; Site-directed mutagenesis; Electrochemistry; Rhodobacter capsulatus; MPT; molybdopterin; DMSO; dimethylsulfoxide; MGD; molybdopterin guanine dinucleotide; NAP; periplasmic nitrate reductase; FDH; formate dehydrogenase; ASO; arsenite oxidase; TMAO; trimethylamine-N-oxide; MV; methyl viologen; DMS; dimethylsulfide; DCPIP; dichlorophenol indophenol; DDAB; didodecyldimethylammonium bromide; CSIRO; Commonwealth Scientific and Industrial Research Organization; ICP-MS; inductively coupled plasma mass spectrometry; | |
| DOI : 10.1016/S0014-5793(04)00301-1 | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
PDF
|
|
【 摘 要 】
In dimethylsulfoxide reductase of Rhodobacter capsulatus tryptophan-116 forms a hydrogen bond with a single oxo ligand bound to the molybdenum ion. Mutation of this residue to phenylalanine affected the UV/visible spectrum of the purified MoVI form of dimethylsulfoxide reductase resulting in the loss of the characteristic transition at 720 nm. Results of steady-state kinetic analysis and electrochemical studies suggest that tryptophan 116 plays a critical role in stabilizing the hexacoordinate monooxo MoVI form of the enzyme and prevents the formation of a dioxo pentacoordinate MoVI species, generated as a consequence of the dissociation of one of the dithiolene ligands of the molybdopterin cofactor from the Mo ion.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020314029ZK.pdf | 129KB |
PDF