Nature of the oxomolybdenum-thiolate pi-bond: implications for Mo-S bonding in sulfite oxidase and xanthine oxidase.
The electronic structure of cis,trans-(L-N(2)S(2))MoO(X) (where L-N(2)S(2) = N,N'-dimethyl-N,N'-bis(2-mercaptophenyl)ethylenediamine and X = Cl, SCH(2)C(6)H(5), SC(6)H(4)-OCH(3), or SC(6)H(4)CF(3)) has been probed by electronic absorption, magnetic circular dichroism, and resonance Raman spectroscopies to determine the nature of oxomolybdenum-thiolate bonding in complexes possessing three equatorial sulfur ligands. One of the phenyl mercaptide sulfur donors of the tetradentate L-N(2)S(2) chelating ligand, denoted S(180), coordinates to molybdenum in the equatorial plane such that the OMo-S(180)-C(phenyl) dihedral angle is approximately 180 degrees, resulting in a highly covalent pi-bonding interaction between an S(180) p orbital and the molybdenum d(xy) orbital. This highly covalent bonding scheme is the origin of an intense low-energy S --> Mo d(xy) bonding-to-antibonding LMCT transition (E(max) approximately 16000 cm(-)(1), epsilon approximately 4000 M(-)(1) cm(-)(1)). Spectroscopically calibrated bonding calculations performed at the DFT level of theory reveal that S(180) contributes approximately 22% to the HOMO, which is predominantly a pi antibonding molecular orbital between Mo d(xy) and the S(180) p orbital oriented in the same plane. The second sulfur donor of the L-N(2)S(2) ligand is essentially nonbonding with Mo d(xy) due to an OMo-S-C(phenyl) dihedral angle of approximately 90 degrees. Because the formal Mo d(xy) orbital is the electroactive or redox orbital, these Mo d(xy)-S 3p interactions are important with respect to defining key covalency contributions to the reduction potential in monooxomolybdenum thiolates, including the one- and two-electron reduced forms of sulfite oxidase. Interestingly, the highly covalent Mo-S(180) pi bonding interaction observed in these complexes is analogous to the well-known Cu-S(Cys) pi bond in type 1 blue copper proteins, which display electronic absorption and resonance Raman spectra that are remarkably similar to these monooxomolybdenum thiolate complexes. Finally, the presence of a covalent Mo-S pi interaction oriented orthogonal to the MOO bond is discussed with respect to electron-transfer regeneration in sulfite oxidase and Mo=S(sulfido) bonding in xanthine oxidase.
Departments of Chemistry, The University of New Mexico, MSC03 2060, 1 University of New Mexico, Albuquerque, New Mexico 87131-0001, USA.
Rebecca L
RL
McNaughton
Matthew E
ME
Helton
Michele Mader
MM
Cosper
John H
JH
Enemark
Martin L
ML
Kirk
D001665:Binding Sites; D002942:Circular Dichroism; D008024:Ligands; D008968:Molecular Conformation; D015394:Molecular Structure; D008982:Molybdenum / Q000737:chemistry*; D009942:Organometallic Compounds / Q000737:chemistry; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000737:chemistry*; D013059:Spectrum Analysis, Raman; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D013455:Sulfur / Q000737:chemistry*; D014969:Xanthine Oxidase / Q000737:chemistry*
D008024:Ligands; D009942:Organometallic Compounds; D013438:Sulfhydryl Compounds; D013455:Sulfur; D008982:Molybdenum; D014969:Xanthine Oxidase; D050862:Oxidoreductases Acting on Sulfur Group Donors