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Volumn 121, Issue 6, 1999, Pages 1256-1266

Structure of the molybdenum site of dimethyl sulfoxide reductase

Author keywords

[No Author keywords available]

Indexed keywords

DIMETHYL SULFIDE; DITHIONITE; MOLYBDENUM; OXIDOREDUCTASE; OXYGEN;

EID: 0033576980     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja982843k     Document Type: Article
Times cited : (156)

References (81)
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    • The EXAFSPAK program suite was developed by G.N.G.
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    • 2 weighting is used (from 0.231 to 0.160). In either case, the intensity of the Mo=O peak in the EXAFS Fourier transform is only reproduced with two Mo=O ligands.
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    • We note that discrimination of four Mo-S ligands from five Mo-S ligands is bordering on the limts of accuracy of the technique, and our coordination numbers discussed above are thus somewhat tentative.
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    • Sulfenic acids (R-S-OH) are chemically unstable and are not known as free acids, but are known mostly from their derivatives, e.g. sulfenyl halides (R-S-Cl). Nevertheless, biological sulfenic acids are known, and in particular a cysteine sulfenic acid is the redox center in streptococcal NADH peroxidase (Stehle, T.; Ahmed, S. A.; Claiborne, A.; Schultz, G. E. J. Mol. Biol. 1991, 221, 1325-1344). The possibility of derivitization of a cofactor dithiolene might provide an expanation for the observations of Bastian et al. (Bastian, N. R.; Foster, M. J. P.; Pope, J. C. Biofactors 1995, 5, 5-10) of modified Mo(V) EPR and optical spectra in the presence of NO and related compounds.
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    • Sulfenic acids (R-S-OH) are chemically unstable and are not known as free acids, but are known mostly from their derivatives, e.g. sulfenyl halides (R-S-Cl). Nevertheless, biological sulfenic acids are known, and in particular a cysteine sulfenic acid is the redox center in streptococcal NADH peroxidase (Stehle, T.; Ahmed, S. A.; Claiborne, A.; Schultz, G. E. J. Mol. Biol. 1991, 221, 1325-1344). The possibility of derivitization of a cofactor dithiolene might provide an expanation for the observations of Bastian et al. (Bastian, N. R.; Foster, M. J. P.; Pope, J. C. Biofactors 1995, 5, 5-10) of modified Mo(V) EPR and optical spectra in the presence of NO and related compounds.
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    • note
    • We note that there is a clear difference between chemically unusual or novel and chemically unreasonable; the active sites of very many metalloproteins can be considered to be chemically unusual.


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