Synthesis and Reactivity Studies of Model Complexes for Molybdopterin-Dependent Enzymes
(2000) In Journal of Inorganic Biochemistry 79(1-4). p.67-74- Abstract
- The molybdenum cofactor (Moco)-containing enzymes are divided into three classes that are named after prototypical members of each family, viz. sulfite oxidase, DMSO reductase and xanthine oxidase. Functional or structural models have been prepared for these three prototypical enzymes: (i) The complex [MoO2(mnt)2]2− (mnt2−=1,2-dicyanoethylenedithiolate) has been found to be able to oxidize hydrogen sulfite to HSO4− and is thus a functional model of sulfite oxidase. Kinetic and computational studies indicate that the reaction proceeds via attack of the substrate at one of the oxo ligands of the complex, rather than at the metal. (ii) The coordination geometries of the mono-oxo [Mo(VI)(O-Ser)(S2)2] entity (S2=dithiolene moiety of... (More)
- The molybdenum cofactor (Moco)-containing enzymes are divided into three classes that are named after prototypical members of each family, viz. sulfite oxidase, DMSO reductase and xanthine oxidase. Functional or structural models have been prepared for these three prototypical enzymes: (i) The complex [MoO2(mnt)2]2− (mnt2−=1,2-dicyanoethylenedithiolate) has been found to be able to oxidize hydrogen sulfite to HSO4− and is thus a functional model of sulfite oxidase. Kinetic and computational studies indicate that the reaction proceeds via attack of the substrate at one of the oxo ligands of the complex, rather than at the metal. (ii) The coordination geometries of the mono-oxo [Mo(VI)(O-Ser)(S2)2] entity (S2=dithiolene moiety of molybdopterin) found in the crystal structure of R. sphaeroides DMSO reductase and the corresponding des-oxo Mo(IV) unit have been reproduced in the complexes [M(VI)O(OSiR3)(bdt)2] and [M(VI)O(OSiR3)(bdt)2] (M=Mo,W; bdt=benzene dithiolate). (iii) A facile route has been developed for the preparation of complexes containing a cis-Mo(VI)OS molybdenum oxo, sulfido moiety similar to that detected in the oxidized form of xanthine oxidase. (Less)
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https://lup.lub.lu.se/record/959665
- author
- Thapper, Anders ; Lorber, Christian ; Fryxelius, Jacob ; Behrens, Axel and Nordlander, Ebbe LU
- organization
- publishing date
- 2000
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Oxotransferase, Molybdenum cofactor, Molybdopterin, Model complexes
- in
- Journal of Inorganic Biochemistry
- volume
- 79
- issue
- 1-4
- pages
- 67 - 74
- publisher
- Elsevier
- external identifiers
-
- scopus:0034732617
- ISSN
- 1873-3344
- DOI
- 10.1016/S0162-0134(00)00010-6
- language
- English
- LU publication?
- yes
- id
- 855008ef-9d8d-4c2a-919d-43cb722cd4c0 (old id 959665)
- date added to LUP
- 2016-04-01 15:53:21
- date last changed
- 2022-01-28 07:49:35
@article{855008ef-9d8d-4c2a-919d-43cb722cd4c0,
abstract = {{The molybdenum cofactor (Moco)-containing enzymes are divided into three classes that are named after prototypical members of each family, viz. sulfite oxidase, DMSO reductase and xanthine oxidase. Functional or structural models have been prepared for these three prototypical enzymes: (i) The complex [MoO2(mnt)2]2− (mnt2−=1,2-dicyanoethylenedithiolate) has been found to be able to oxidize hydrogen sulfite to HSO4− and is thus a functional model of sulfite oxidase. Kinetic and computational studies indicate that the reaction proceeds via attack of the substrate at one of the oxo ligands of the complex, rather than at the metal. (ii) The coordination geometries of the mono-oxo [Mo(VI)(O-Ser)(S2)2] entity (S2=dithiolene moiety of molybdopterin) found in the crystal structure of R. sphaeroides DMSO reductase and the corresponding des-oxo Mo(IV) unit have been reproduced in the complexes [M(VI)O(OSiR3)(bdt)2] and [M(VI)O(OSiR3)(bdt)2] (M=Mo,W; bdt=benzene dithiolate). (iii) A facile route has been developed for the preparation of complexes containing a cis-Mo(VI)OS molybdenum oxo, sulfido moiety similar to that detected in the oxidized form of xanthine oxidase.}},
author = {{Thapper, Anders and Lorber, Christian and Fryxelius, Jacob and Behrens, Axel and Nordlander, Ebbe}},
issn = {{1873-3344}},
keywords = {{Oxotransferase; Molybdenum cofactor; Molybdopterin; Model complexes}},
language = {{eng}},
number = {{1-4}},
pages = {{67--74}},
publisher = {{Elsevier}},
series = {{Journal of Inorganic Biochemistry}},
title = {{Synthesis and Reactivity Studies of Model Complexes for Molybdopterin-Dependent Enzymes}},
url = {{http://dx.doi.org/10.1016/S0162-0134(00)00010-6}},
doi = {{10.1016/S0162-0134(00)00010-6}},
volume = {{79}},
year = {{2000}},
}