Monooxomolybdenum(VI) complexes possessing olefinic dithiolene ligands: probing Mo-S covalency contributions to electron transfer in dimethyl sulfoxide reductase family molybdoenzymes.
A monooxomolybdenum(VI) model complex for the oxidized active site in the DMSOR family of molybdoenzymes has been synthesized and structurally characterized. The compound was obtained from the desoxomolybdenum(IV) derivative by clean oxygen-atom transfer from an amine N-oxide in a manner similar to that observed in the enzyme. A combination of electronic absorption and resonance Raman spectroscopies, coupled with the results of bonding and excited-state calculations, has been used to provide strong support for a highly covalent Mo(d(xy))-S(dithiolene) pi*-bonding interaction in the molybdenum(VI) complex. It is proposed that the resulting Mo-S covalency facilitates electron-transfer regeneration of the catalytically competent DMSOR Mo(IV) active site.
Sugimoto
Hideki
H
Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan. sugimoto@mls.eng.osaka-u.ac.jp
Tatemoto
Susumu
S
Suyama
Koichiro
K
Miyake
Hiroyuki
H
Mtei
Regina P
RP
Itoh
Shinobu
S
Kirk
Martin L
ML
D000475:Alkenes / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004583:Electrons; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D008982:Molybdenum / Q000737:chemistry*; D009942:Organometallic Compounds / Q000138:chemical synthesis* / Q000737:chemistry; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D013438:Sulfhydryl Compounds / Q000737:chemistry*
D000475:Alkenes; D007506:Iron-Sulfur Proteins; D008024:Ligands; D009942:Organometallic Compounds; D013438:Sulfhydryl Compounds; D008982:Molybdenum; D010088:Oxidoreductases; C045664:dimethyl sulfoxide reductase